8HGN
Crystal structure of MeaC (Mesaconyl-CoA hydratase)
Summary for 8HGN
| Entry DOI | 10.2210/pdb8hgn/pdb |
| Descriptor | Beta-methylmalyl-CoA dehydratase, D-MALATE (3 entities in total) |
| Functional Keywords | lyase |
| Biological source | Methylorubrum extorquens CM4 |
| Total number of polymer chains | 1 |
| Total formula weight | 38985.72 |
| Authors | |
| Primary citation | Ahn, J.W.,Hong, J.,Kim, K.J. Crystal Structure of Mesaconyl-CoA Hydratase from Methylorubrum extorquens CM4. J Microbiol Biotechnol., 33:485-492, 2023 Cited by PubMed Abstract: , a facultative methylotroph, assimilates C compounds and accumulates poly-β-hydroxylbutyrate (PHB) as carbon and energy sources. The ethylmalonyl pathway is central to the carbon metabolism of , 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 (MeaC) that catalyzes the reversible conversion of mesaconyl-CoA to β-methylmalyl-CoA. The crystal structure of MeaC revealed that the enzyme belongs to the MaoC-like dehydratase domain superfamily and functions as a trimer. In our current MeaC structure, malic acid occupied the substrate binding site, which reveals how MeaC recognizes the β-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. PubMed: 36788474DOI: 10.4014/jmb.2212.12003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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