6h9e
From Proteopedia
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<StructureSection load='6h9e' size='340' side='right'caption='[[6h9e]], [[Resolution|resolution]] 1.82Å' scene=''> | <StructureSection load='6h9e' size='340' side='right'caption='[[6h9e]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6h9e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H9E OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6h9e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H9E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=FWK:(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-ethyl-oxolane-3,4-diol'>FWK</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=FWK:(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-ethyl-oxolane-3,4-diol'>FWK</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</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=6h9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h9e OCA], [https://pdbe.org/6h9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h9e RCSB], [https://www.ebi.ac.uk/pdbsum/6h9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h9e ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/GMSS_CLOCO GMSS_CLOCO] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526]<ref>PMID:1315276</ref> <ref>PMID:7880251</ref> <ref>PMID:8013871</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Catalysis by radical enzymes dependent on coenzyme B12 (AdoCbl) relies on the reactive primary 5'-deoxy-5'adenosyl radical, which originates from reversible Co-C bond homolysis of AdoCbl. This bond homolysis is accelerated roughly 10(12) -fold upon binding the enzyme substrate. The structural basis for this activation is still strikingly enigmatic. As revealed here, a displaced firm adenosine binding cavity in substrate-loaded glutamate mutase (GM) causes a structural misfit for intact AdoCbl that is relieved by the homolytic Co-C bond cleavage. Strategically interacting adjacent adenosine- and substrate-binding protein cavities provide a tight caged radical reaction space, controlling the entire radical path. The GM active site is perfectly structured for promoting radical catalysis, including "negative catalysis", a paradigm for AdoCbl-dependent mutases. | ||
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| + | Structure-Based Demystification of Radical Catalysis by a Coenzyme B12 Dependent Enzyme-Crystallographic Study of Glutamate Mutase with Cofactor Homologues.,Gruber K, Csitkovits V, Lyskowski A, Kratky C, Krautler B Angew Chem Int Ed Engl. 2022 Aug 26;61(35):e202208295. doi:, 10.1002/anie.202208295. Epub 2022 Jul 21. PMID:35793207<ref>PMID:35793207</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6h9e" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Clostridium cochlearium]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Csitkovits V]] | |
| - | [[Category: Csitkovits | + | [[Category: Gruber K]] |
| - | [[Category: Gruber | + | [[Category: Kratky C]] |
| - | [[Category: Kratky | + | |
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Revision as of 06:20, 26 October 2022
Structure of glutamate mutase reconstituted with homo-coenzyme B12
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