3ojo

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<StructureSection load='3ojo' size='340' side='right'caption='[[3ojo]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3ojo' size='340' side='right'caption='[[3ojo]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ojo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OJO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ojo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OJO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EU:EUROPIUM+ION'>EU</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PDC:PYRIDINE-2,6-DICARBOXYLIC+ACID'>PDC</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ojl|3ojl]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EU:EUROPIUM+ION'>EU</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PDC:PYRIDINE-2,6-DICARBOXYLIC+ACID'>PDC</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cap5O ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ojo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ojo OCA], [https://pdbe.org/3ojo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ojo RCSB], [https://www.ebi.ac.uk/pdbsum/3ojo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ojo 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=3ojo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ojo OCA], [https://pdbe.org/3ojo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ojo RCSB], [https://www.ebi.ac.uk/pdbsum/3ojo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ojo 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/P95708_STAAU P95708_STAAU]
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Bacterial UDP-sugar dehydrogenases are part of the biosynthesis pathway of extracellular polysaccharides. These compounds act as important virulence factors by protecting the cell from opsonophagocytosis and complement-mediated killing. In Staphylococcus aureus, the protein Cap5O catalyzes the oxidation of UDP-N-acetyl-mannosamine to UDP-N-acetyl-mannosaminuronic acid. Cap5O is crucial for the production of serotype 5 capsular polysaccharide that prevents the interaction of bacteria with both phagocytic and nonphagocytic eukaryotic cells. However, details of its catalytic mechanism remain unknown. We thus crystallized Cap5O and solved the first structure of an UDP-N-acetyl-mannosamine dehydrogenase. This study revealed that the catalytic cysteine makes a disulfide bond that has never been observed in other structurally characterized members of the NDP-sugar dehydrogenase family. Biochemical and mutagenesis experiments demonstrated that the formation of this disulfide bridge regulates the activity of Cap5O. We also identified two arginine residues essential for Cap5O activity. Previous data suggested that Cap5O is activated by tyrosine phosphorylation, so we characterized the phosphorylation site and examined the underlying regulatory mechanism.
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Structure analysis of the staphylococcus aureus UDP-N-acetyl-mannosamine dehydrogenase Cap5O involved in capsular polysaccharide biosynthesis.,Gruszczyk J, Fleurie A, Olivares-Illana V, Bechet E, Zanella-Cleon I, Morera S, Meyer P, Pompidor G, Kahn R, Grangeasse C, Nessler S J Biol Chem. 2011 Mar 23. PMID:21454499<ref>PMID:21454499</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 3ojo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gruszczyk, J]]
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[[Category: Staphylococcus aureus]]
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[[Category: Meyer, P]]
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[[Category: Gruszczyk J]]
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[[Category: Morera, S]]
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[[Category: Meyer P]]
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[[Category: Nessler, S]]
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[[Category: Morera S]]
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[[Category: Olivares-Illana, V]]
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[[Category: Nessler S]]
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[[Category: Oxidized conformation]]
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[[Category: Olivares-Illana V]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Revision as of 11:16, 21 February 2024

Derivative structure of the UDP-N-acetyl-mannosamine dehydrogenase Cap5O from S. aureus

PDB ID 3ojo

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