1cvr

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spinqualitylabelsall models 1cvr, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE ARG SPECIFIC CYSTEINE PROTEINASE GINGIPAIN R (RGPB)

Overview

Gingipains are cysteine proteinases acting as key virulence factors of the, bacterium Porphyromonas gingivalis, the major pathogen in periodontal, disease. The 1.5 and 2.0 A crystal structures of free and, D-Phe-Phe-Arg-chloromethylketone-inhibited gingipain R reveal a, 435-residue, single-polypeptide chain organized into a catalytic and an, immunoglobulin-like domain. The catalytic domain is subdivided into two, subdomains comprising four- and six-stranded beta-sheets sandwiched by, alpha-helices. Each subdomain bears topological similarities to the, p20-p10 heterodimer of caspase-1. The second subdomain harbours the, Cys-His catalytic diad and a nearby Glu arranged around the S1 specificity, pocket, which carries an Asp residue to enforce preference for Arg-P1, residues. This gingipain R structure is an excellent template for the, rational design of drugs with a potential to cure and prevent, periodontitis. Here we show the binding mode of an arginine-containing, inhibitor in the active-site, thus identifying major interaction sites, defining a suitable pharmacophor.

About this Structure

1CVR is a Single protein structure of sequence from Porphyromonas gingivalis with CA and ZN as ligands. Active as Gingipain R, with EC number 3.4.22.37 Full crystallographic information is available from OCA.

Reference

Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold., Eichinger A, Beisel HG, Jacob U, Huber R, Medrano FJ, Banbula A, Potempa J, Travis J, Bode W, EMBO J. 1999 Oct 15;18(20):5453-62. PMID:10523290

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