7pld

Caulobacter crescentus xylonolactonase with (R)-4-hydroxy-2-pyrrolidone

spinqualitylabelsall models 7pld, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7pld is a 2 chain structure with sequence from Caulobacter vibrioides CB15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: 7UK, FE2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function XYLC_CAUVC Involved in the degradation of D-xylose (PubMed:22709678, PubMed:25073011). Catalyzes the hydrolysis of D-xylonolactone to D-xylonate (PubMed:25073011, PubMed:34633186). Publication Abstract from PubMed Xylonolactonase Cc XylC from Caulobacter crescentus catalyzes the hydrolysis of the intramolecular ester bond of d-xylonolactone. We have determined crystal structures of Cc XylC in complex with d-xylonolactone isomer analogues d-xylopyranose and (r)-(+)-4-hydroxy-2-pyrrolidinone at high resolution. Cc XylC has a 6-bladed beta-propeller architecture, which contains a central open channel having the active site at one end. According to our previous native mass spectrometry studies, Cc XylC is able to specifically bind Fe(2+) . The crystal structures, presented here, revealed an active site bound metal ion with an octahedral binding geometry. The side chains of three amino acid residues, Glu18, Asn146, and Asp196, which participate in binding of metal ion are located in the same plane. The solved complex structures allowed suggesting a reaction mechanism for intramolecular ester bond hydrolysis in which the major contribution for catalysis arises from the carbonyl oxygen coordination of the xylonolactone substrate to the Fe(2+) . The structure of Cc XylC was compared with eight other ester hydrolases of the beta-propeller hydrolase family. The previously published crystal structures of other beta-propeller hydrolases contain either Ca(2+) , Mg(2+) , or Zn(2+) and show clear similarities in ligand and metal ion binding geometries to that of Cc XylC. It would be interesting to reinvestigate the metal binding specificity of these enzymes and clarify whether they are also able to use Fe(2+) as a catalytic metal. This could further expand our understanding of utilization of Fe(2+) not only in oxidative enzymes but also in hydrolases. Three-dimensional structure of xylonolactonase from Caulobacter crescentus: A mononuclear iron enzyme of the 6-bladed beta-propeller hydrolase family.,Paakkonen J, Hakulinen N, Andberg M, Koivula A, Rouvinen J Protein Sci. 2021 Nov 11. doi: 10.1002/pro.4229. PMID:34761460 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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