4ETW

Structure of the Enzyme-ACP Substrate Gatekeeper Complex Required for Biotin Synthesis

4ETW の概要

• エントリーDOI: 10.2210/pdb4etw/pdb
• 分子名称: Pimelyl-[acyl-carrier protein] methyl ester esterase, Acyl carrier protein, methyl 7-{[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]sulfanyl}-7-oxoheptanoate, ... (4 entities in total)
• 機能のキーワード: esterase, hydrolase
• 由来する生物種: Shigella flexneri; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 77241.80

構造登録者

Agarwal, V.,Nair, S.K. (登録日: 2012-04-24, 公開日: 2012-10-17, 最終更新日: 2024-10-30)

主引用文献

Agarwal, V.,Lin, S.,Lukk, T.,Nair, S.K.,Cronan, J.E.
Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis.
Proc.Natl.Acad.Sci.USA, 109:17406-17411, 2012

PubMed Abstract: Although the pimeloyl moiety was long known to be a biotin precursor, the mechanism of assembly of this C7 α,ω-dicarboxylic acid was only recently elucidated. In Escherichia coli, pimelate is made by bypassing the strict specificity of the fatty acid synthetic pathway. BioC methylates the free carboxyl of a malonyl thioester, which replaces the usual acetyl thioester primer. This atypical primer is transformed to pimeloyl-acyl carrier protein (ACP) methyl ester by two cycles of fatty acid synthesis. The question is, what stops this product from undergoing further elongation? Although BioH readily cleaves this product in vitro, the enzyme is nonspecific, which made assignment of its physiological substrate problematical, especially because another enzyme, BioF, could also perform this gatekeeping function. We report the 2.05-Å resolution cocrystal structure of a complex of BioH with pimeloyl-ACP methyl ester and use the structure to demonstrate that BioH is the gatekeeper and its physiological substrate is pimeloyl-ACP methyl ester.

PubMed: 23045647
DOI: 10.1073/pnas.1207028109

実験手法

X-RAY DIFFRACTION (2.05 Å)