한빛사 논문
Hanseong Kim1, Sojin An1, Yeo Reum Park2, Hara Jang2, Heeseon Yoo2, Sang Ho Park1, Seung Jae Lee2,* and Uhn-Soo Cho1,*
1 Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
2 Department of Chemistry, Chonbuk National University, Jeonju 54896, Republic of Korea.
*Corresponding author : Seung Jae Lee, Uhn-Soo Cho
Abstract
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. Here, 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 dissociation with Fe1 coordination. Furthermore, 1,6-hexanediol, a mimic of the products of sMMO, reveals the substrate access route.
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