8hgn
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of MeaC (Mesaconyl-CoA hydratase)== | |
| + | <StructureSection load='8hgn' size='340' side='right'caption='[[8hgn]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8hgn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens_CM4 Methylorubrum extorquens CM4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HGN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</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=8hgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hgn OCA], [https://pdbe.org/8hgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hgn RCSB], [https://www.ebi.ac.uk/pdbsum/8hgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hgn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B7KZU4_METC4 B7KZU4_METC4] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Methylorubrum extorquens, a facultative methylotroph, assimilates C(1) compounds and accumulates poly-beta-hydroxylbutyrate (PHB) as carbon and energy sources. The ethylmalonyl pathway is central to the carbon metabolism of M. extorquens, and is linked with a serine cycle and a PHB biosynthesis pathway. Understanding the ethylmalonyl pathway is vital in utilizing methylotrophs to produce value-added chemicals. In this study, we determined the crystal structure of the mesaconyl-CoA hydratase from M. extorquens (MeMeaC) that catalyzes the reversible conversion of mesaconyl-CoA to beta-methylmalyl-CoA. The crystal structure of MeMeaC revealed that the enzyme belongs to the MaoC-like dehydratase domain superfamily and functions as a trimer. In our current MeMeaC structure, malic acid occupied the substrate binding site, which reveals how MeMeaC recognizes the beta-methylmalyl-moiety of its substrate. The active site of the enzyme was further speculated by comparing its structure with those of other MaoC-like hydratases. | ||
| - | + | Crystal Structure of Mesaconyl-CoA Hydratase from Methylorubrum extorquens CM4.,Ahn JW, Hong J, Kim KJ J Microbiol Biotechnol. 2023 Apr 28;33(4):485-492. doi: 10.4014/jmb.2212.12003. , Epub 2023 Jan 26. PMID:36788474<ref>PMID:36788474</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8hgn" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methylorubrum extorquens CM4]] | ||
| + | [[Category: Ahn JW]] | ||
| + | [[Category: Hong J]] | ||
| + | [[Category: Kim KJ]] | ||
Current revision
Crystal structure of MeaC (Mesaconyl-CoA hydratase)
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