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  • 1
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    Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-06-19
    Description: Archaeal and eukaryotic translation elongation factor 2 contain a unique post-translationally modified histidine residue called diphthamide, which is the target of diphtheria toxin. The biosynthesis of diphthamide was proposed to involve three steps, with the first being the formation of a C-C bond between the histidine residue and the 3-amino-3-carboxypropyl group of S-adenosyl-l-methionine (SAM). However, further details of the biosynthesis remain unknown. Here we present structural and biochemical evidence showing that the first step of diphthamide biosynthesis in the archaeon Pyrococcus horikoshii uses a novel iron-sulphur-cluster enzyme, Dph2. Dph2 is a homodimer and each of its monomers can bind a [4Fe-4S] cluster. Biochemical data suggest that unlike the enzymes in the radical SAM superfamily, Dph2 does not form the canonical 5'-deoxyadenosyl radical. Instead, it breaks the C(gamma,Met)-S bond of SAM and generates a 3-amino-3-carboxypropyl radical. Our results suggest that P. horikoshii Dph2 represents a previously unknown, SAM-dependent, [4Fe-4S]-containing enzyme that catalyses unprecedented chemistry.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3006227/" 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/PMC3006227/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Yang -- Zhu, Xuling -- Torelli, Andrew T -- Lee, Michael -- Dzikovski, Boris -- Koralewski, Rachel M -- Wang, Eileen -- Freed, Jack -- Krebs, Carsten -- Ealick, Steven E -- Lin, Hening -- P41 RR016292/RR/NCRR NIH HHS/ -- P41 RR016292-01/RR/NCRR NIH HHS/ -- P41 RR016292-09/RR/NCRR NIH HHS/ -- P41 RR016292-10/RR/NCRR NIH HHS/ -- P41 RR016292-11/RR/NCRR NIH HHS/ -- P41-RR016292/RR/NCRR NIH HHS/ -- R01 GM088276/GM/NIGMS NIH HHS/ -- R01 GM088276-01/GM/NIGMS NIH HHS/ -- R01GM088276/GM/NIGMS NIH HHS/ -- RR-15301/RR/NCRR NIH HHS/ -- England -- Nature. 2010 Jun 17;465(7300):891-6. doi: 10.1038/nature09138.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20559380" target="_blank"〉PubMed〈/a〉
    Keywords: Archaeal Proteins/*metabolism ; Free Radicals/chemistry/*metabolism ; Histidine/*analogs & derivatives/biosynthesis/chemistry ; Iron-Sulfur Proteins/*metabolism ; Pyrococcus horikoshii/*enzymology ; S-Adenosylmethionine/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Protein crystal growth in microgravity (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-03
    Description: The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. space shuttle flight STS-26 in September 1988. The microgravity-grown crystals of gamma-interferon D1, porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on Earth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeLucas, L J -- Smith, C D -- Smith, H W -- Vijay-Kumar, S -- Senadhi, S E -- Ealick, S E -- Carter, D C -- Snyder, R S -- Weber, P C -- Salemme, F R -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):651-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Alabama, Center for Macromolecular Crystallography, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2510297" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallization ; Interferon-gamma ; Isocitrate Lyase ; Pancreatic Elastase ; *Proteins ; Space Flight ; Swine ; *Weightlessness
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Three-dimensional structure of recombinant human interferon-gamma (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: The x-ray crystal structure of recombinant human interferon-gamma has been determined with the use of multiple-isomorphous-replacement techniques. Interferon-gamma, which is dimeric in solution, crystallizes with two dimers related by a noncrystallographic twofold axis in the asymmetric unit. The protein is primarily alpha helical, with six helices in each subunit that comprise approximately 62 percent of the structure; there is no beta sheet. The dimeric structure of human interferon-gamma is stabilized by the intertwining of helices across the subunit interface with multiple intersubunit interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ealick, S E -- Cook, W J -- Vijay-Kumar, S -- Carson, M -- Nagabhushan, T L -- Trotta, P P -- Bugg, C E -- CA-13148/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):698-702.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Alabama, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902591" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallization ; Glycosylation ; Humans ; Interferon-gamma/*chemistry ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Recombinant Proteins ; Sequence Homology, Nucleic Acid ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-10-28
    Description: Thiamine pyrophosphate 1 is an essential cofactor in all living systems. Its biosynthesis involves the separate syntheses of the pyrimidine 2 and thiazole 3 precursors, which are then coupled. Two biosynthetic routes to the thiamine thiazole have been identified. In prokaryotes, five enzymes act on three substrates to produce the thiazole via a complex oxidative condensation reaction, the mechanistic details of which are now well established. In contrast, only one gene product is involved in thiazole biosynthesis in eukaryotes (THI4p in Saccharomyces cerevisiae). Here we report the preparation of fully active recombinant wild-type THI4p, the identification of an iron-dependent sulphide transfer reaction from a conserved cysteine residue of the protein to a reaction intermediate and the demonstration that THI4p is a suicide enzyme undergoing only a single turnover.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3205460/" 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/PMC3205460/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chatterjee, Abhishek -- Abeydeera, N Dinuka -- Bale, Shridhar -- Pai, Pei-Jing -- Dorrestein, Pieter C -- Russell, David H -- Ealick, Steven E -- Begley, Tadhg P -- DK44083/DK/NIDDK NIH HHS/ -- DK67081/DK/NIDDK NIH HHS/ -- R01 DK067081/DK/NIDDK NIH HHS/ -- R37 DK044083/DK/NIDDK NIH HHS/ -- R37 DK044083-21/DK/NIDDK NIH HHS/ -- England -- Nature. 2011 Oct 26;478(7370):542-6. doi: 10.1038/nature10503.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22031445" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Biocatalysis ; Carbon-Nitrogen Lyases/chemistry/*metabolism ; Conserved Sequence ; Cysteine/metabolism ; Iron/metabolism ; Molecular Sequence Data ; Recombinant Proteins ; Saccharomyces cerevisiae/*enzymology ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Sulfides/metabolism ; Sulfur/metabolism ; Thiamine/*metabolism ; Thiamine Pyrophosphate/metabolism ; Thiazoles/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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