5TV6

A. aeolicus BioW with pimelate

5TV6 の概要

• エントリーDOI: 10.2210/pdb5tv6/pdb
• 関連するPDBエントリー: 5TV5 5TV8 5TVA
• 分子名称: 6-carboxyhexanoate--CoA ligase, PIMELIC ACID (3 entities in total)
• 機能のキーワード: pimeloyl-coa ligase, adenylation, ligase
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55681.05

構造登録者

Estrada, P.,Manandhar, M.,Dong, S.-H.,Deveryshetty, J.,Agarwal, V.,Cronan, J.E.,Nair, S.K. (登録日: 2016-11-08, 公開日: 2016-12-07, 最終更新日: 2024-10-30)

主引用文献

Estrada, P.,Manandhar, M.,Dong, S.H.,Deveryshetty, J.,Agarwal, V.,Cronan, J.E.,Nair, S.K.
The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes.
Nat. Chem. Biol., 13:668-674, 2017

PubMed Abstract: Reactions that activate carboxylates through acyl-adenylate intermediates are found throughout biology and include acyl- and aryl-CoA synthetases and tRNA synthetases. Here we describe the characterization of Aquifex aeolicus BioW, which represents a new protein fold within the superfamily of adenylating enzymes. Substrate-bound structures identified the enzyme active site and elucidated the mechanistic strategy for conjugating CoA to the seven-carbon α,ω-dicarboxylate pimelate, a biotin precursor. Proper position of reactive groups for the two half-reactions is achieved solely through movements of active site residues, as confirmed by site-directed mutational analysis. The ability of BioW to hydrolyze adenylates of noncognate substrates is reminiscent of pre-transfer proofreading observed in some tRNA synthetases, and we show that this activity can be abolished by mutation of a single residue. These studies illustrate how BioW can carry out three different biologically prevalent chemical reactions (adenylation, thioesterification, and proofreading) in the context of a new protein fold.

PubMed: 28414711
DOI: 10.1038/nchembio.2359

実験手法

X-RAY DIFFRACTION (2.456 Å)