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  • 1
    Publication Date: 1999-10-03
    Description: Precursors of alpha-defensin peptides require activation for bactericidal activity. In mouse small intestine, matrilysin colocalized with alpha-defensins (cryptdins) in Paneth cell granules, and in vitro it cleaved the pro segment from cryptdin precursors. Matrilysin-deficient (MAT-/-) mice lacked mature cryptdins and accumulated precursor molecules. Intestinal peptide preparations from MAT-/- mice had decreased antimicrobial activity. Orally administered bacteria survived in greater numbers and were more virulent in MAT-/- mice than in MAT+/+ mice. Thus, matrilysin functions in intestinal mucosal defense by regulating the activity of defensins, which may be a common role for this metalloproteinase in its numerous epithelial sites of expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, C L -- Ouellette, A J -- Satchell, D P -- Ayabe, T -- Lopez-Boado, Y S -- Stratman, J L -- Hultgren, S J -- Matrisian, L M -- Parks, W C -- New York, N.Y. -- Science. 1999 Oct 1;286(5437):113-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Division of Allergy and Pulmonary Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA. wilson_c@kids.wustl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10506557" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Catalysis ; Cytoplasmic Granules/enzymology ; Escherichia coli/growth & development ; Escherichia coli Infections/immunology/microbiology ; Female ; Humans ; *Immunity, Innate ; *Immunity, Mucosal ; Intestinal Mucosa/enzymology/immunology/microbiology ; Intestine, Small/enzymology/*immunology/microbiology ; Male ; Matrix Metalloproteinase 7 ; Metalloendopeptidases/genetics/*metabolism ; Mice ; Molecular Sequence Data ; Paneth Cells/enzymology ; Protein Precursors/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Salmonella typhimurium/growth & development/pathogenicity ; Tissue Extracts/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 2
    Publication Date: 1999-08-14
    Description: Many Gram-negative pathogens assemble architecturally and functionally diverse adhesive pili on their surfaces by the chaperone-usher pathway. Immunoglobulin-like periplasmic chaperones escort pilus subunits to the usher, a large protein complex that facilitates the translocation and assembly of subunits across the outer membrane. The crystal structure of the PapD-PapK chaperone-subunit complex, determined at 2.4 angstrom resolution, reveals that the chaperone functions by donating its G(1) beta strand to complete the immunoglobulin-like fold of the subunit via a mechanism termed donor strand complementation. The structure of the PapD-PapK complex also suggests that during pilus biogenesis, every subunit completes the immunoglobulin-like fold of its neighboring subunit via a mechanism termed donor strand exchange.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sauer, F G -- Futterer, K -- Pinkner, J S -- Dodson, K W -- Hultgren, S J -- Waksman, G -- R01AI29549/AI/NIAID NIH HHS/ -- R01DK51406/DK/NIDDK NIH HHS/ -- R01GM54033/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):1058-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10446050" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/*metabolism ; Crystallography, X-Ray ; Escherichia coli ; *Escherichia coli Proteins ; Fimbriae Proteins ; Fimbriae, Bacterial/chemistry/*metabolism/ultrastructure ; Models, Molecular ; Molecular Chaperones/*chemistry/*metabolism ; Molecular Sequence Data ; *Periplasmic Proteins ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Sequence Alignment
    Print ISSN: 0036-8075
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-08-19
    Description: Bacteria that are engulfed by phagocytic cells of the immune system are usually destroyed once inside the host cell but not always. Why is it that sometimes engulfed bacteria survive and thrive quite happily inside the host cell? As Mulvey and Hultgren explain in their Perspective, the answer may lie in small indentations in the host cell plasma membrane called caveolae that direct certain signal transduction pathways inside the host cell (Shin et al.). If bacteria adhere to regions of the host cell surface that is rich in caveolae, they are better able to survive once inside the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mulvey, M A -- Hultgren, S J -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):732-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110-1093, USA. mulvey@borcim.wustl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10950716" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/metabolism ; *Adhesins, Escherichia coli ; Animals ; Antigens, CD/metabolism ; Bacterial Adhesion ; Caveolin 1 ; *Caveolins ; Cell Membrane/chemistry/*metabolism/microbiology/ultrastructure ; *Endocytosis ; Escherichia coli/*metabolism/pathogenicity ; *Fimbriae Proteins ; Glycosylphosphatidylinositols/metabolism ; Macrophages/microbiology ; Mast Cells/metabolism/*microbiology/ultrastructure ; Membrane Proteins/analysis ; Mice ; Signal Transduction
    Print ISSN: 0036-8075
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  • 4
    Publication Date: 2002-02-02
    Description: Amyloid is associated with debilitating human ailments including Alzheimer's and prion diseases. Biochemical, biophysical, and imaging analyses revealed that fibers produced by Escherichia coli called curli were amyloid. The CsgA curlin subunit, purified in the absence of the CsgB nucleator, adopted a soluble, unstructured form that upon prolonged incubation assembled into fibers that were indistinguishable from curli. In vivo, curli biogenesis was dependent on the nucleation-precipitation machinery requiring the CsgE and CsgF chaperone-like and nucleator proteins, respectively. Unlike eukaryotic amyloid formation, curli biogenesis is a productive pathway requiring a specific assembly machinery.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838482/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838482/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chapman, Matthew R -- Robinson, Lloyd S -- Pinkner, Jerome S -- Roth, Robyn -- Heuser, John -- Hammar, Marten -- Normark, Staffan -- Hultgren, Scott J -- 1 F32 AI10502-01A1/AI/NIAID NIH HHS/ -- AI29549/AI/NIAID NIH HHS/ -- AI48689/AI/NIAID NIH HHS/ -- DK51406/DK/NIDDK NIH HHS/ -- F32 AI010502/AI/NIAID NIH HHS/ -- F32 AI010502-03/AI/NIAID NIH HHS/ -- NIA P50 AG05681-17/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):851-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Microbial Pathogenesis, Box 8230, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823641" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/genetics/metabolism/ultrastructure ; Amyloid/chemistry/*metabolism/ultrastructure ; Bacterial Proteins/chemistry/genetics/*metabolism/ultrastructure ; Biopolymers ; Circular Dichroism ; Congo Red/metabolism ; Escherichia coli/genetics/*metabolism ; Escherichia coli Proteins/chemistry/genetics/*metabolism/ultrastructure ; Mutation ; *Operon ; Protein Structure, Secondary ; Protein Subunits
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  • 5
    Publication Date: 1999-08-14
    Description: Type 1 pili-adhesive fibers expressed in most members of the Enterobacteriaceae family-mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choudhury, D -- Thompson, A -- Stojanoff, V -- Langermann, S -- Pinkner, J -- Hultgren, S J -- Knight, S D -- R01AI29549/AI/NIAID NIH HHS/ -- R01DK51406/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):1061-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Uppsala Biomedical Center, Swedish University of Agricultural Sciences, Box 590, S-753 24 Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10446051" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/*chemistry/metabolism ; *Adhesins, Escherichia coli ; Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/metabolism ; *Bacterial Proteins ; Chlorpropamide/analogs & derivatives/metabolism ; Crystallography, X-Ray ; Escherichia coli/*chemistry/metabolism/pathogenicity ; *Escherichia coli Proteins ; Fimbriae Proteins ; Fimbriae, Bacterial/chemistry/*metabolism/ultrastructure ; Hydrogen Bonding ; Membrane Proteins/*chemistry ; Models, Molecular ; Molecular Chaperones/*chemistry/metabolism ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Sequence Alignment
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  • 6
    Publication Date: 1997-04-25
    Description: Virtually all uropathogenic strains of Escherichia coli, the primary cause of cystitis, assemble adhesive surface organelles called type 1 pili that contain the FimH adhesin. Sera from animals vaccinated with candidate FimH vaccines inhibited uropathogenic E. coli from binding to human bladder cells in vitro. Immunization with FimH reduced in vivo colonization of the bladder mucosa by more than 99 percent in a murine cystitis model, and immunoglobulin G to FimH was detected in urinary samples from protected mice. Furthermore, passive systemic administration of immune sera to FimH also resulted in reduced bladder colonization by uropathogenic E. coli. This approach may represent a means of preventing recurrent and acute infections of the urogenital mucosa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langermann, S -- Palaszynski, S -- Barnhart, M -- Auguste, G -- Pinkner, J S -- Burlein, J -- Barren, P -- Koenig, S -- Leath, S -- Jones, C H -- Hultgren, S J -- R01DK51406/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):607-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MedImmune, Inc., Gaithersburg, MD 20878, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9110982" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/*immunology/metabolism ; *Adhesins, Escherichia coli ; Animals ; Antibodies, Bacterial/analysis/immunology ; Bacterial Adhesion ; *Bacterial Vaccines/administration & dosage/immunology ; Child ; Cystitis/immunology/*prevention & control ; Epithelium/microbiology ; Escherichia coli/immunology/metabolism/pathogenicity ; Escherichia coli Infections/immunology/*prevention & control ; Female ; *Fimbriae Proteins ; Fimbriae, Bacterial/immunology ; Humans ; Immunity, Mucosal ; Mice ; Mice, Inbred C3H ; Neutrophils/immunology ; Rabbits ; Urinary Bladder/microbiology ; Vaccination ; *Vaccines, Synthetic/administration & dosage/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 7
    Publication Date: 2003-07-05
    Description: Escherichia coli entry into the bladder is met with potent innate defenses, including neutrophil influx and epithelial exfoliation. Bacterial subversion of innate responses involves invasion into bladder superficial cells. We discovered that the intracellular bacteria matured into biofilms, creating pod-like bulges on the bladder surface. Pods contained bacteria encased in a polysaccharide-rich matrix surrounded by a protective shell of uroplakin. Within the biofilm, bacterial structures interacted extensively with the surrounding matrix, and biofilm associated factors had regional variation in expression. The discovery of intracellular biofilm-like pods explains how bladder infections can persist in the face of robust host defenses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, Gregory G -- Palermo, Joseph J -- Schilling, Joel D -- Roth, Robyn -- Heuser, John -- Hultgren, Scott J -- AI29549/AI/NIAID NIH HHS/ -- AI48689/AI/NIAID NIH HHS/ -- DK51406/DK/NIDDK NIH HHS/ -- DK64540/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 4;301(5629):105-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12843396" target="_blank"〉PubMed〈/a〉
    Keywords: *Adhesins, Bacterial ; Adhesins, Escherichia coli ; Animals ; *Antigens, Bacterial ; Bacterial Outer Membrane Proteins/analysis ; *Biofilms ; Colony Count, Microbial ; Epithelial Cells/microbiology/ultrastructure ; Escherichia coli/growth & development/immunology/*pathogenicity/ultrastructure ; Escherichia coli Infections/immunology/*microbiology/pathology ; *Escherichia coli Proteins ; Female ; Fimbriae, Bacterial/physiology/ultrastructure ; Freeze Fracturing ; Immunity, Innate ; Membrane Glycoproteins/analysis ; Mice ; Mice, Inbred C3H ; Microscopy, Electron ; Microscopy, Electron, Scanning ; Polysaccharides, Bacterial/analysis ; Urinary Bladder/immunology/*microbiology/ultrastructure ; Urinary Bladder Diseases/immunology/*microbiology/pathology ; Urinary Tract Infections/immunology/*microbiology/pathology ; Urothelium/microbiology/ultrastructure
    Print ISSN: 0036-8075
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  • 8
    Publication Date: 1998-11-20
    Description: Virtually all uropathogenic strains of Escherichia coli encode filamentous surface adhesive organelles called type 1 pili. High-resolution electron microscopy of infected mouse bladders revealed that type 1 pilus tips interacted directly with the lumenal surface of the bladder, which is embedded with hexagonal arrays of integral membrane glycoproteins known as uroplakins. Attached pili were shortened and facilitated intimate contact of the bacteria with the uroplakin-coated host cells. Bacterial attachment resulted in exfoliation of host bladder epithelial cells as part of an innate host defense system. Exfoliation occurred through a rapid apoptosis-like mechanism involving caspase activation and host DNA fragmentation. Bacteria resisted clearance in the face of host defenses within the bladder by invading into the epithelium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mulvey, M A -- Lopez-Boado, Y S -- Wilson, C L -- Roth, R -- Parks, W C -- Heuser, J -- Hultgren, S J -- AI09787/AI/NIAID NIH HHS/ -- R01AI29549/AI/NIAID NIH HHS/ -- R01DK51406/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1494-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Microbial Pathogenesis, Box 8230, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9822381" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/metabolism ; *Adhesins, Escherichia coli ; Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; Apoptosis ; Bacterial Adhesion ; Caspase Inhibitors ; Caspases/metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Cystitis/*microbiology/pathology ; DNA Fragmentation ; Escherichia coli/genetics/*pathogenicity ; Escherichia coli Infections/*microbiology/pathology ; Female ; *Fimbriae Proteins ; Fimbriae, Bacterial/physiology/ultrastructure ; In Situ Nick-End Labeling ; Membrane Glycoproteins/analysis/metabolism ; Mice ; Mice, Inbred C57BL ; Microscopy, Electron ; Microscopy, Electron, Scanning ; Tetraspanins ; Urinary Bladder/chemistry/*microbiology/pathology ; Uroplakin Ib ; Urothelium/microbiology/pathology
    Print ISSN: 0036-8075
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  • 9
    Publication Date: 2011-06-04
    Description: Type 1 pili are the archetypal representative of a widespread class of adhesive multisubunit fibres in Gram-negative bacteria. During pilus assembly, subunits dock as chaperone-bound complexes to an usher, which catalyses their polymerization and mediates pilus translocation across the outer membrane. Here we report the crystal structure of the full-length FimD usher bound to the FimC-FimH chaperone-adhesin complex and that of the unbound form of the FimD translocation domain. The FimD-FimC-FimH structure shows FimH inserted inside the FimD 24-stranded beta-barrel translocation channel. FimC-FimH is held in place through interactions with the two carboxy-terminal periplasmic domains of FimD, a binding mode confirmed in solution by electron paramagnetic resonance spectroscopy. To accommodate FimH, the usher plug domain is displaced from the barrel lumen to the periplasm, concomitant with a marked conformational change in the beta-barrel. The amino-terminal domain of FimD is observed in an ideal position to catalyse incorporation of a newly recruited chaperone-subunit complex. The FimD-FimC-FimH structure provides unique insights into the pilus subunit incorporation cycle, and captures the first view of a protein transporter in the act of secreting its cognate substrate.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3162478/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3162478/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Phan, Gilles -- Remaut, Han -- Wang, Tao -- Allen, William J -- Pirker, Katharina F -- Lebedev, Andrey -- Henderson, Nadine S -- Geibel, Sebastian -- Volkan, Ender -- Yan, Jun -- Kunze, Micha B A -- Pinkner, Jerome S -- Ford, Bradley -- Kay, Christopher W M -- Li, Huilin -- Hultgren, Scott J -- Thanassi, David G -- Waksman, Gabriel -- 29549/PHS HHS/ -- 48689/PHS HHS/ -- 49950/PHS HHS/ -- 85602/Medical Research Council/United Kingdom -- BB/F001134/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G0100442/Medical Research Council/United Kingdom -- G0100442(58149)/Medical Research Council/United Kingdom -- G0800002/Medical Research Council/United Kingdom -- GM62987/GM/NIGMS NIH HHS/ -- GM74985/GM/NIGMS NIH HHS/ -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 GM062987/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Jun 2;474(7349):49-53. doi: 10.1038/nature10109.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21637253" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Escherichia coli/*chemistry/metabolism ; Crystallization ; Escherichia coli Proteins/*chemistry/metabolism ; Fimbriae Proteins/*chemistry/metabolism ; *Models, Molecular ; Protein Binding ; Protein Structure, Quaternary
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
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  • 10
    Publication Date: 2013-04-13
    Description: Type 1 pili, produced by uropathogenic Escherichia coli, are multisubunit fibres crucial in recognition of and adhesion to host tissues. During pilus biogenesis, subunits are recruited to an outer membrane assembly platform, the FimD usher, which catalyses their polymerization and mediates pilus secretion. The recent determination of the crystal structure of an initiation complex provided insight into the initiation step of pilus biogenesis resulting in pore activation, but very little is known about the elongation steps that follow. Here, to address this question, we determine the structure of an elongation complex in which the tip complex assembly composed of FimC, FimF, FimG and FimH passes through FimD. This structure demonstrates the conformational changes required to prevent backsliding of the nascent pilus through the FimD pore and also reveals unexpected properties of the usher pore. We show that the circular binding interface between the pore lumen and the folded substrate participates in transport by defining a low-energy pathway along which the nascent pilus polymer is guided during secretion.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3673227/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3673227/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geibel, Sebastian -- Procko, Erik -- Hultgren, Scott J -- Baker, David -- Waksman, Gabriel -- 85602/Medical Research Council/United Kingdom -- AI029549/AI/NIAID NIH HHS/ -- G0800002/Medical Research Council/United Kingdom -- G0800002(85602)/Medical Research Council/United Kingdom -- P41 GM103533/GM/NIGMS NIH HHS/ -- P41GM103533/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2013 Apr 11;496(7444):243-6. doi: 10.1038/nature12007.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23579681" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/*metabolism ; Fimbriae Proteins/*chemistry/*metabolism ; Fimbriae, Bacterial/chemistry/metabolism ; Models, Molecular ; Protein Conformation ; *Protein Folding ; Protein Stability ; Protein Transport ; Thermodynamics
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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