초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 09월 10일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 MMOD-induced structural changes of hydroxylase in soluble methane monooxygenase

2019년 8월 29일 12시 57분 11초
LIFE.O-4 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
목 09시 : 45분
Life Chemistry - Oral Presentations by Young Life Chemists
저자 및
Hanseong Kim, Minseok Kwak, Seung Jae Lee1, Uhn-Soo Cho2,*
Department of Chemistry, Pukyong National University, Korea
1Department of Chemistry, Chonbuk National University, Korea
2Department of Biological Chemistry, University of Michigan, U.S.A., United States
※ 국외소속으로 등록된 저자의 승인여부는 최소 3일이내 발표자 email로 알려드립니다.
승인 1건

Soluble methane monooxygenase in methanotrophs converts methane to methanol under ambient conditions. The maximum catalytic activity of hydroxylase (MMOH) is achieved through the interplay of its regulatory protein (MMOB) and reductase. An additional auxiliary protein, MMOD, functions as an inhibitor of MMOH; however, its inhibitory mechanism remains unknown. Herein, we report the crystal structure of the MMOH–MMOD complex from Methylosinus sporium strain 5 (2.6 Å). Its structure illustrates that MMOD associates with the canyon region of MMOH where MMOB binds. Although MMOD and MMOB recognize the same binding site, each binding component triggers different conformational changes toward MMOH, which then respectively lead to the inhibition and activation of MMOH. Particularly, MMOD binding perturbs the di-iron geometry by inducing two major MMOH conformational changes, i.e., MMOH β-subunit disorganization and subsequent His147 dissociate with on Fe1 coordination. Furthermore, 1,6-hexanediol, a mimic of the products of sMMO, reveals the substrate access route.