Journal of Microbiology and Biotechnology

  • 제33권4호
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  • Pages.485-492
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  • 2023
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
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Crystal Structure of Mesaconyl-CoA Hydratase from Methylorubrum extorquens CM4

  • Jae-Woo Ahn (Postech Biotech Center, Pohang University of Science and Technology) ;
  • Jiyeon Hong (School of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, KNU Institute for Microorganisms, Kyungpook National University) ;
  • Kyung-Jin Kim (School of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, KNU Institute for Microorganisms, Kyungpook National University)
  • 투고 : 2022.12.02
  • 심사 : 2023.01.18
  • 발행 : 2023.04.28
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초록

Methylorubrum extorquens, a facultative methylotroph, assimilates C1 compounds and accumulates poly-β-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 β-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 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.

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과제정보

This work was supported by the Cooperative Research Program for Agricultural Science & Technology Development (Project No. PJ01492602), Rural Development Administration, Republic of Korea, and also by the National Research Foundation of Korea (NRF) grant funded by the Korean government (MIST, No. 2021R1C1C2004411); JW Ahn was supported by the Basic Science Research Program (No. 2020R1I1A1A01057880) and the Korea Initiative for fostering University of Research and Innovation Program (No.2020M3H1A1075314) through the National Research Foundation of Korea (NRF) funded by the Korean government.

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