8FHJ

Crystal structure of a FAD monooxygenease from Methylocystis sp. Strain SB2

8FHJ の概要

• エントリーDOI: 10.2210/pdb8fhj/pdb
• 分子名称: Monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: methanobactin, biosynthetic protein
• 由来する生物種: Methylocystis sp. SB2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 185130.95

構造登録者

Stewart, A.M.,Sawaya, M.R.,Stewart, C.E. (登録日: 2022-12-14, 公開日: 2023-05-03, 最終更新日: 2024-05-22)

主引用文献

Stewart, A.,Dershwitz, P.,Stewart Jr., C.,Sawaya, M.R.,Yeates, T.O.,Semrau, J.D.,Zischka, H.,DiSpirito, A.A.,Bobik, T.A.
Crystal structure of MbnF: an NADPH-dependent flavin monooxygenase from Methylocystis strain SB2.
Acta Crystallogr.,Sect.F, 79:111-118, 2023

PubMed Abstract: Methanobactins (MBs) are ribosomally produced and post-translationally modified peptides (RiPPs) that are used by methanotrophs for copper acquisition. The signature post-translational modification of MBs is the formation of two heterocyclic groups, either an oxazolone, pyrazinedione or imidazolone group, with an associated thioamide from an X-Cys dipeptide. The precursor peptide (MbnA) for MB formation is found in a gene cluster of MB-associated genes. The exact biosynthetic pathway of MB formation is not yet fully understood, and there are still uncharacterized proteins in some MB gene clusters, particularly those that produce pyrazinedione or imidazolone rings. One such protein is MbnF, which is proposed to be a flavin monooxygenase (FMO) based on homology. To help to elucidate its possible function, MbnF from Methylocystis sp. strain SB2 was recombinantly produced in Escherichia coli and its X-ray crystal structure was resolved to 2.6 Å resolution. Based on its structural features, MbnF appears to be a type A FMO, most of which catalyze hydroxylation reactions. Preliminary functional characterization shows that MbnF preferentially oxidizes NADPH over NADH, supporting NAD(P)H-mediated flavin reduction, which is the initial step in the reaction cycle of several type A FMO enzymes. It is also shown that MbnF binds the precursor peptide for MB, with subsequent loss of the leader peptide sequence as well as the last three C-terminal amino acids, suggesting that MbnF might be needed for this process to occur. Finally, molecular-dynamics simulations revealed a channel in MbnF that is capable of accommodating the core MbnA fragment minus the three C-terminal amino acids.

PubMed: 37158309
DOI: 10.1107/S2053230X23003035

実験手法

X-RAY DIFFRACTION (2.61 Å)