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'''Unreleased structure'''


The entry 8hgn is ON HOLD  until Paper Publication
==Crystal structure of MeaC (Mesaconyl-CoA hydratase)==
<StructureSection load='8hgn' size='340' side='right'caption='[[8hgn]], [[Resolution|resolution]] 1.95&Aring;' 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]] 1.95&#8491;</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.


Authors: Ahn, J.W., Hong, J., Kim, K.J.
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>


Description: Crystal structure of MeaC (Mesaconyl-CoA hydratase)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Hong, J]]
<div class="pdbe-citations 8hgn" style="background-color:#fffaf0;"></div>
[[Category: Kim, K.J]]
== References ==
[[Category: Ahn, J.W]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylorubrum extorquens CM4]]
[[Category: Ahn JW]]
[[Category: Hong J]]
[[Category: Kim KJ]]
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