2w8s

CRYSTAL STRUCTURE OF A catalytically promiscuous PHOSPHONATE MONOESTER HYDROLASE FROM Burkholderia caryophylli

spinqualitylabelsall models 2w8s, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w8s is a 4 chain structure with sequence from Trinickia caryophylli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: FE, FGL, GOL, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BCPMH_TRICW Hydrolytic enzyme with a broad substrate specificity acting on phosphate diesters and phosphonate monoesters (PubMed:20133613, PubMed:8824203). Hydrolyzes phosphate mono- and triesters, sulfate monoesters and sulfonate monoesters (PubMed:20133613). Hydrolyzes glyphosate monoesters. Does not hydrolyze DNA or cGMP (PubMed:8824203). Hydrolyzes glyceryl glyphosate, but this substrate has a much lower affinity than the glyphosate monoesters (PubMed:8771792, PubMed:8824203). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We report a catalytically promiscuous enzyme able to efficiently promote the hydrolysis of six different substrate classes. Originally assigned as a phosphonate monoester hydrolase (PMH) this enzyme exhibits substantial second-order rate accelerations ((k(cat)/K(M))/k(w)), ranging from 10(7) to as high as 10(19), for the hydrolyses of phosphate mono-, di-, and triesters, phosphonate monoesters, sulfate monoesters, and sulfonate monoesters. This substrate collection encompasses a range of substrate charges between 0 and -2, transition states of a different nature, and involves attack at two different reaction centers (P and S). Intrinsic reactivities (half-lives) range from 200 days to 10(5) years under near neutrality. The substantial rate accelerations for a set of relatively difficult reactions suggest that efficient catalysis is not necessarily limited to efficient stabilization of just one transition state. The crystal structure of PMH identifies it as a member of the alkaline phosphatase superfamily. PMH encompasses four of the native activities previously observed in this superfamily and extends its repertoire by two further activities, one of which, sulfonate monoesterase, has not been observed previously for a natural enzyme. PMH is thus one of the most promiscuous hydrolases described to date. The functional links between superfamily activities can be presumed to have played a role in functional evolution by gene duplication. An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily.,van Loo B, Jonas S, Babtie AC, Benjdia A, Berteau O, Hyvonen M, Hollfelder F Proc Natl Acad Sci U S A. 2010 Feb 16;107(7):2740-5. Epub 2010 Jan 27. PMID:20133613 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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