ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
Cryo-EM Structures Reveal the Molecular Basis of Asymmetric Allosteric Activation by MMOB in the Hydroxylase of Soluble Methane Monooxygenase.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Soluble methane monooxygenase (sMMO) catalyzes the hydroxylation of methane at non-heme di-iron active sites under ambient conditions. The regulatory component (MMOB) is essential for catalytic activity, inducing conformational changes in the active site and facilitating substrate ingress in hydroxylase (MMOH). Advances in cryogenic electron microscopy (cryo-EM) have enabled structural studies of sMMO under near-native conditions. 3D variability analysis reveals that an asymmetric MMOH-MMOB complex predominates in solution, supporting a sequential binding mechanism. Here, we report a 2.85 Å-resolution cryo-EM structure of MMOH-1MMOB (H-1B) complex, in which a single MMOB binds to MMOH and generates two distinct protomers: MMOB-bound protomer (HB
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