6D7K

Complex structure of Methane monooxygenase hydroxylase in complex with inhibitory subunit

Summary for 6D7K

• Entry DOI: 10.2210/pdb6d7k/pdb
• Descriptor: Methane monooxygenase hydroxylase, MmoX1, Methane monooxygenase hydroxylase, MmoY, Methane monooxygenase hydroxylase, MmoZ, ... (8 entities in total)
• Functional Keywords: complex, oxidoreductase, oxidoreductase-inhibitor complex, oxidoreductase/inhibitor
• Biological source: Methylosinus sporium; More
• Total number of polymer chains: 8
• Total formula weight: 275497.42

Authors

Kim, H.,Lee, S.J.,Cho, U.-S. (deposition date: 2018-04-24, release date: 2019-06-26, Last modification date: 2023-10-04)

Primary citation

Kim, H.,An, S.,Park, Y.R.,Jang, H.,Yoo, H.,Park, S.H.,Lee, S.J.,Cho, U.S.
MMOD-induced structural changes of hydroxylase in soluble methane monooxygenase.
Sci Adv, 5:eaax0059-eaax0059, 2019

PubMed 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 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 His dissociation with Fe1 coordination. Furthermore, 1,6-hexanediol, a mimic of the products of sMMO, reveals the substrate access route.

PubMed: 31616787
DOI: 10.1126/sciadv.aax0059

Experimental method

X-RAY DIFFRACTION (2.6 Å)