7us5

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<StructureSection load='7us5' size='340' side='right'caption='[[7us5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='7us5' size='340' side='right'caption='[[7us5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7us5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7US5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7US5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7us5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7US5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7US5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7us5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7us5 OCA], [https://pdbe.org/7us5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7us5 RCSB], [https://www.ebi.ac.uk/pdbsum/7us5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7us5 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7us5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7us5 OCA], [https://pdbe.org/7us5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7us5 RCSB], [https://www.ebi.ac.uk/pdbsum/7us5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7us5 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/Q5M6Q7_CAMJU Q5M6Q7_CAMJU]]
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Campylobacter jejuni is a human pathogen and a leading cause of food poisoning in the United States and Europe. Surrounding the outside of the bacterium is a carbohydrate coat known as the capsular polysaccharide. Various strains of C. jejuni have different sequences of unusual sugars and an assortment of decorations. Many of the serotypes have heptoses with differing stereochemical arrangements at C2 through C6. One of the many common modifications is a 6-deoxy-heptose that is formed by dehydration of GDP-d-glycero-alpha-d-manno-heptose to GDP-6-deoxy-4-keto-d-lyxo-heptose via the action of the enzyme GDP-d-glycero-alpha-d-manno-heptose 4,6-dehydratase. Herein, we report the biochemical and structural characterization of this enzyme from C. jejuni 81-176 (serotype HS:23/36). The enzyme was purified to homogeneity, and its three-dimensional structure was determined to a resolution of 2.1 A. Kinetic analyses suggest that the reaction mechanism proceeds through the formation of a 4-keto intermediate followed by the loss of water from C5/C6. Based on the three-dimensional structure, it is proposed that oxidation of C4 is assisted by proton transfer from the hydroxyl group to the phenolate of Tyr-159 and hydride transfer to the tightly bound NAD(+) in the active site. Elimination of water at C5/C6 is most likely assisted by abstraction of the proton at C5 by Glu-136 and subsequent proton transfer to the hydroxyl at C6 via Ser-134 and Tyr-159. A bioinformatic analysis identified 19 additional 4,6-dehydratases from serotyped strains of C. jejuni that are 89-98% identical in the amino acid sequence, indicating that each of these strains should contain a 6-deoxy-heptose within their capsular polysaccharides.
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Reaction Mechanism and Three-Dimensional Structure of GDP-d-glycero-alpha-d-manno-heptose 4,6-Dehydratase from Campylobacter jejuni.,Xiang DF, Thoden JB, Ghosh MK, Holden HM, Raushel FM Biochemistry. 2022 Jul 5;61(13):1313-1322. doi: 10.1021/acs.biochem.2c00244. Epub, 2022 Jun 17. PMID:35715226<ref>PMID:35715226</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7us5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Campylobacter jejuni]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Holden, H M]]
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[[Category: Holden HM]]
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[[Category: Raushel, F M]]
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[[Category: Raushel FM]]
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[[Category: Thoden, J B]]
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[[Category: Thoden JB]]
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[[Category: Xiang, D F]]
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[[Category: Xiang DF]]
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[[Category: Capsular polysaccharide]]
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[[Category: Dehydratase]]
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[[Category: Oxidoreductase]]
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Revision as of 06:26, 8 September 2022

X-ray crystal structure of GDP-D-glycero-D-manno-heptose 4,6-Dehydratase from Campylobacter jejuni

PDB ID 7us5

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