4M7S

Crystal structure of SeMet BtrN in an OPEN conformation

4M7S の概要

• エントリーDOI: 10.2210/pdb4m7s/pdb
• 関連するPDBエントリー: 4M7T
• 分子名称: BtrN, IRON/SULFUR CLUSTER, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: adomet radical fold, metal binding protein
• 由来する生物種: Bacillus circulans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32032.42

構造登録者

Goldman, P.J.,Drennan, C.L. (登録日: 2013-08-12, 公開日: 2013-10-02, 最終更新日: 2024-10-30)

主引用文献

Goldman, P.J.,Grove, T.L.,Booker, S.J.,Drennan, C.L.
X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry.
Proc.Natl.Acad.Sci.USA, 110:15949-15954, 2013

PubMed Abstract: The 2-deoxy-scyllo-inosamine (DOIA) dehydrogenases are key enzymes in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. In contrast to most DOIA dehydrogenases, which are NAD-dependent, the DOIA dehydrogenase from Bacillus circulans (BtrN) is an S-adenosyl-l-methionine (AdoMet) radical enzyme. To examine how BtrN employs AdoMet radical chemistry, we have determined its structure with AdoMet and substrate to 1.56 Å resolution. We find a previously undescribed modification to the core AdoMet radical fold: instead of the canonical (β/α)6 architecture, BtrN displays a (β5/α4) motif. We further find that an auxiliary [4Fe-4S] cluster in BtrN, thought to bind substrate, is instead implicated in substrate-radical oxidation. High structural homology in the auxiliary cluster binding region between BtrN, fellow AdoMet radical dehydrogenase anSME, and molybdenum cofactor biosynthetic enzyme MoaA provides support for the establishment of an AdoMet radical structural motif that is likely common to ~6,400 uncharacterized AdoMet radical enzymes.

PubMed: 24048029
DOI: 10.1073/pnas.1312228110

実験手法

X-RAY DIFFRACTION (2.022 Å)