3WL5

Crystal structure of pOPH S172C

3WL5 の概要

• エントリーDOI: 10.2210/pdb3wl5/pdb
• 関連するPDBエントリー: 3WL6 3WL7 3WL8 3WLA
• 分子名称: Oxidized polyvinyl alcohol hydrolase, CITRIC ACID (3 entities in total)
• 機能のキーワード: alpha/beta-hydrolase, oxi-polyvinyl alcohol hydrolase, hydrolase
• 由来する生物種: Pseudomonas sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39520.91

構造登録者

Yang, Y.,Ko, T.P.,Li, J.H.,Liu, L.,Huang, C.H.,Chan, H.C.,Ren, F.F.,Jia, D.X.,Wang, A.H.-J.,Guo, R.T.,Chen, J.,Du, G.C. (登録日: 2013-11-07, 公開日: 2014-09-24, 最終更新日: 2017-11-22)

主引用文献

Yang, Y.,Ko, T.P.,Liu, L.,Li, J.,Huang, C.H.,Chan, H.C.,Ren, F.,Jia, D.,Wang, A.H.-J.,Guo, R.T.,Chen, J.,Du, G.
Structural insights into enzymatic degradation of oxidized polyvinyl alcohol
Chembiochem, 15:1882-1886, 2014

PubMed Abstract: The ever-increasing production and use of polyvinyl alcohol (PVA) threaten our environment. Yet PVA can be assimilated by microbes in two steps: oxidation and cleavage. Here we report novel α/β-hydrolase structures of oxidized PVA hydrolase (OPH) from two known PVA-degrading organisms, Sphingopyxis sp. 113P3 and Pseudomonas sp. VM15C, including complexes with substrate analogues, acetylacetone and caprylate. The active site is covered by a lid-like β-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the CC bond of β-diketone, although it has a catalytic triad similar to that of most α/β-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving β-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications.

PubMed: 25044912
DOI: 10.1002/cbic.201402166

実験手法

X-RAY DIFFRACTION (1.6 Å)