7xrm
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Ethanolamine ammonia-lyase complexed with AdoMeCbl== | |
| + | <StructureSection load='7xrm' size='340' side='right'caption='[[7xrm]], [[Resolution|resolution]] 2.13Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7xrm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XRM FirstGlance]. <br> | ||
| + | </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=NH4:AMMONIUM+ION'>NH4</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=7xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xrm OCA], [https://pdbe.org/7xrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xrm RCSB], [https://www.ebi.ac.uk/pdbsum/7xrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xrm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The X-ray structures of coenzyme B(12) (AdoCbl)-dependent eliminating isomerases complexed with adenosylmethylcobalamin (AdoMeCbl) have been determined. As judged from geometries, the Co-C bond in diol dehydratase (DD) is not activated even in the presence of substrate. In ethanolamine ammonia-lyase (EAL), the bond is elongated in the absence of substrate; in the presence of substrate, the complex likely exists in both pre- and post-homolysis states. The impacts of incorporating an extra CH(2) group are different in the two enzymes: the DD active site is flexible, and AdoMeCbl binding causes large conformational changes that make DD unable to adopt the catalytic state, whereas the EAL active site is rigid, and AdoMeCbl binding does not induce significant conformational changes. Such flexibility and rigidity of the active sites might reflect the tightness of adenine binding. The structures provide good insights into the basis of the very low activity of AdoMeCbl in these enzymes. | ||
| - | + | Structural Insights into the Very Low Activity of the Homocoenzyme B(12) Adenosylmethylcobalamin in Coenzyme B(12) -Dependent Diol Dehydratase and Ethanolamine Ammonia-Lyase.,Shibata N, Higuchi Y, Krautler B, Toraya T Chemistry. 2022 Nov 21;28(65):e202202196. doi: 10.1002/chem.202202196. Epub 2022 , Sep 19. PMID:35974426<ref>PMID:35974426</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Shibata | + | <div class="pdbe-citations 7xrm" style="background-color:#fffaf0;"></div> |
| - | [[Category: Toraya | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Shibata N]] | ||
| + | [[Category: Toraya T]] | ||
Revision as of 06:42, 29 March 2023
Ethanolamine ammonia-lyase complexed with AdoMeCbl
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