3WL5
Crystal structure of pOPH S172C
Summary for 3WL5
| Entry DOI | 10.2210/pdb3wl5/pdb |
| Related | 3WL6 3WL7 3WL8 3WLA |
| Descriptor | Oxidized polyvinyl alcohol hydrolase, CITRIC ACID (3 entities in total) |
| Functional Keywords | alpha/beta-hydrolase, oxi-polyvinyl alcohol hydrolase, hydrolase |
| Biological source | Pseudomonas sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 39520.91 |
| 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: 2013-11-07, release date: 2014-09-24, Last modification date: 2017-11-22) |
| Primary citation | 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 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 CC 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: 25044912DOI: 10.1002/cbic.201402166 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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