2jbv
From Proteopedia
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<StructureSection load='2jbv' size='340' side='right'caption='[[2jbv]], [[Resolution|resolution]] 1.86Å' scene=''> | <StructureSection load='2jbv' size='340' side='right'caption='[[2jbv]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2jbv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2jbv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JBV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FAO:[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl+(2R,3S,4S)-5-[(4aS,10aR)-7,8-dimethyl-2,4-dioxo-1,3,4,4a,5,10a-hexahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl+dihydrogen+diphosphate'>FAO</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FAO:[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl+(2R,3S,4S)-5-[(4aS,10aR)-7,8-dimethyl-2,4-dioxo-1,3,4,4a,5,10a-hexahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl+dihydrogen+diphosphate'>FAO</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=2jbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbv OCA], [https://pdbe.org/2jbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jbv RCSB], [https://www.ebi.ac.uk/pdbsum/2jbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jbv 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=2jbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbv OCA], [https://pdbe.org/2jbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jbv RCSB], [https://www.ebi.ac.uk/pdbsum/2jbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jbv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/CHOX_ARTGO CHOX_ARTGO] Catalyzes the two-step oxidative conversion of choline to glycine-betaine with betaine aldehyde as an intermediate. Glycine-betaine accumulates to high levels in the cytoplasm of cells to prevent dehydration and plasmolysis in adverse hyperosmotic environments. Accepts either choline or the reaction intermediate betaine-aldehyde as substrate.<ref>PMID:12795615</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Arthrobacter globiformis]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Fan | + | [[Category: Fan F]] |
| - | [[Category: Gadda | + | [[Category: Gadda G]] |
| - | [[Category: Lountos | + | [[Category: Lountos GT]] |
| - | [[Category: Orville | + | [[Category: Orville AM]] |
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Revision as of 14:42, 13 December 2023
Crystal structure of choline oxidase reveals insights into the catalytic mechanism
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