4WGF

YcaC from Pseudomonas aeruginosa with hexane-2,5-diol and covalent acrylamide

4WGF の概要

• エントリーDOI: 10.2210/pdb4wgf/pdb
• 関連するPDBエントリー: 4WH0
• 分子名称: Probable hydrolase, PROPIONAMIDE, (2R,5R)-hexane-2,5-diol, ... (6 entities in total)
• 機能のキーワード: co-purified, hydrolase, parallel beta-sheet, contaminant.
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 184119.50

構造登録者

Groftehauge, M.K.,Truan, D.,Vasil, A.,Denny, P.W.,Vasil, M.L.,Pohl, E. (登録日: 2014-09-18, 公開日: 2015-07-29, 最終更新日: 2024-11-20)

主引用文献

Grftehauge, M.K.,Truan, D.,Vasil, A.,Denny, P.W.,Vasil, M.L.,Pohl, E.
Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct.
Int J Mol Sci, 16:15971-15984, 2015

PubMed Abstract: As part of the ongoing effort to functionally and structurally characterize virulence factors in the opportunistic pathogen Pseudomonas aeruginosa, we determined the crystal structure of YcaC co-purified with the target protein at resolutions of 2.34 and 2.56 Å without a priori knowledge of the protein identity or experimental phases. The three-dimensional structure of YcaC adopts a well-known cysteine hydrolase fold with the putative active site residues conserved. The active site cysteine is covalently bound to propionamide in one crystal form, whereas the second form contains an S-mercaptocysteine. The precise biological function of YcaC is unknown; however, related prokaryotic proteins have functions in antibacterial resistance, siderophore production and NADH biosynthesis. Here, we show that YcaC is exceptionally well conserved across both bacterial and fungal species despite being non-ubiquitous. This suggests that whilst YcaC may not be part of an integral pathway, the function could confer a significant evolutionary advantage to microbial life.

PubMed: 26184183
DOI: 10.3390/ijms160715971

実験手法

X-RAY DIFFRACTION (2.34020690848 Å)