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3WLA

Crystal Structure of sOPH Native

Summary for 3WLA
Entry DOI10.2210/pdb3wla/pdb
Related3WL5 3WL6 3WL7 3WL8
DescriptorOxidized polyvinyl alcohol hydrolase, SULFATE ION (3 entities in total)
Functional Keywordsalpha/beta-hydrolase, oxi-polyvinyl alcohol hydrolase, hydrolase
Biological sourceSphingopyxis
Cellular locationPeriplasm : Q588Z2
Total number of polymer chains3
Total formula weight110001.52
Authors
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. (deposition date: 2013-11-08, release date: 2014-09-24, Last modification date: 2024-11-20)
Primary citationYang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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