8HGN

Crystal structure of MeaC (Mesaconyl-CoA hydratase)

8HGN の概要

• エントリーDOI: 10.2210/pdb8hgn/pdb
• 分子名称: Beta-methylmalyl-CoA dehydratase, D-MALATE (3 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: Methylorubrum extorquens CM4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38985.72

構造登録者

Ahn, J.W.,Hong, J.,Kim, K.J. (登録日: 2022-11-15, 公開日: 2023-09-27)

主引用文献

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

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: 36788474
DOI: 10.4014/jmb.2212.12003

実験手法

X-RAY DIFFRACTION (1.95 Å)