Publication Date:
2006-06-03
Description:
The cytoplasmic membrane protein TonB spans the periplasm of the Gram-negative bacterial cell envelope, contacts cognate outer membrane receptors, and facilitates siderophore transport. The outer membrane receptor FhuA from Escherichia coli mediates TonB-dependent import of ferrichrome. We report the 3.3 angstrom resolution crystal structure of the TonB carboxyl-terminal domain in complex with FhuA. TonB contacts stabilize FhuA's amino-terminal residues, including those of the consensus Ton box sequence that form an interprotein beta sheet with TonB through strand exchange. The highly conserved TonB residue arginine-166 is oriented to form multiple contacts with the FhuA cork, the globular domain enclosed by the beta barrel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pawelek, Peter D -- Croteau, Nathalie -- Ng-Thow-Hing, Christopher -- Khursigara, Cezar M -- Moiseeva, Natalia -- Allaire, Marc -- Coulton, James W -- New York, N.Y. -- Science. 2006 Jun 2;312(5778):1399-402.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec, H3A 2B4, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16741125" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Outer Membrane Proteins/*chemistry/metabolism
;
Crystallography, X-Ray
;
Escherichia coli/*chemistry/metabolism
;
Escherichia coli Proteins/*chemistry/metabolism
;
Ferric Compounds/metabolism
;
Membrane Proteins/*chemistry/metabolism
;
Models, Molecular
;
Protein Binding
;
Protein Conformation
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Surface Plasmon Resonance
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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