3wl7 | pdb_00003wl7

The complex structure of pOPH S172C with ligand, ACA

spinqualitylabelsall models 3wl7, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wl7 is a 1 chain structure with sequence from Pseudomonas sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.67Å Ligands: CIT, OCS, P2D Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OPH_PSESP Publication Abstract from PubMed 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 alpha/beta-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 beta-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the CC bond of beta-diketone, although it has a catalytic triad similar to that of most alpha/beta-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving beta-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications. Structural insights into enzymatic degradation of oxidized polyvinyl alcohol.,Yang Y, Ko TP, Liu L, Li J, Huang CH, Chan HC, Ren F, Jia D, Wang AH, Guo RT, Chen J, Du G Chembiochem. 2014 Sep 5;15(13):1882-6. doi: 10.1002/cbic.201402166. Epub 2014 Jul, 8. PMID:25044912 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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