1azw
From Proteopedia
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PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI
Overview
The proline iminopeptidase from Xanthomonas campestris pv. citri is a, serine peptidase that catalyses the removal of N-terminal proline residues, from peptides with high specificity. We have solved its three-dimensional, structure by multiple isomorphous replacement and refined it to a, crystallographic R-factor of 19.2% using X-ray data to 2.7 A resolution., The protein is folded into two contiguous domains. The larger domain shows, the general topology of the alpha/beta hydrolase fold, with a central, eight-stranded beta-sheet flanked by two helices and the 11 N-terminal, residues on one side, and by four helices on the other side. The smaller, domain is placed on top of the larger domain and essentially consists of, six helices. The active site, located at the end of a deep pocket at the, interface between both domains, includes a catalytic triad of Ser110, Asp266 and His294. Cys269, located at the bottom of the active site very, close to the catalytic triad, presumably accounts for the inhibition by, thiol-specific reagents. The overall topology of this iminopeptidase is, very similar to that of yeast serine carboxypeptidase. The striking, secondary structure similarity to human lymphocytic prolyl oligopeptidase, and dipeptidyl peptidase IV makes this proline iminopeptidase structure a, suitable model for the three-dimensional structure of other peptidases of, this family.
About this Structure
1AZW is a Single protein structure of sequence from Xanthomonas citri. Active as Prolyl aminopeptidase, with EC number 3.4.11.5 Structure known Active Site: AS. Full crystallographic information is available from OCA.
Reference
Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family., Medrano FJ, Alonso J, Garcia JL, Romero A, Bode W, Gomis-Ruth FX, EMBO J. 1998 Jan 2;17(1):1-9. PMID:9427736
Page seeded by OCA on Mon Nov 5 15:52:54 2007
