2fuk
From Proteopedia
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Crystal structure of XC6422 from Xanthomonas campestris: a member of a/b serine hydrolase without lid at 1.6 resolution
Overview
XC6422 is a conserved hypothetical protein from Xanthomonas campestris, pathovar campestris (Xcc), a Gram-negative yellow-pigmented pathogenic, bacterium that causes black rot, one of the major worldwide diseases of, cruciferous crops. The protein consists of 220 amino acids and its, structure has been determined to 1.6 A resolution using the, multi-wavelength anomalous dispersion (MAD) method. Although it has very, low sequence identity to protein sequences in the PDB (less than 20%), the, determined structure nevertheless shows that it belongs to the superfamily, of serine alpha/beta-hydrolases, with an active site that is fully, accessible to solvent owing to the absence of a lid domain. Modelling, studies with the serine esterase inhibitor E600 indicate that XC6422, adopts a conserved Ser-His-Asp catalytic triad common to this superfamily, and has a preformed oxyanion hole for catalytic activation. These, structural features suggest that XC6422 is most likely to be a hydrolase, active on a soluble ester or a small lipid. An extra strand preceding the, first beta-strand in the canonical alpha/beta-hydrolase fold leads to, extensive subunit interactions between XC6422 monomers, which may explain, why XC6422 crystals of good diffraction quality can grow to dimensions of, up to 1.5 mm in a few days.
About this Structure
2FUK is a Protein complex structure of sequences from Xanthomonas campestris. Full crystallographic information is available from OCA.
Reference
Structure of XC6422 from Xanthomonas campestris at 1.6 A resolution: a small serine alpha/beta-hydrolase., Yang CY, Chin KH, Chou CC, Wang AH, Chou SH, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):498-503. Epub 2006 May 31. PMID:16754966
Page seeded by OCA on Tue Jan 29 19:44:53 2008
