1x9y
From Proteopedia
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The prostaphopain B structure
Overview
Prostaphopain B is the precursor of staphopain B, a papain-type secreted, cysteine protease from the pathogen Staphylococcus aureus. Here, we, describe the 2.5 A crystal structure of the proenzyme. Its 21 kDa, proregion is organized around a central half-barrel or barrel-sandwich, hybrid and occludes primed, but not nonprimed, sites in the active site, cleft of the protease. The structure of the mature part of the protease is, similar to previously reported staphopain structures, and no distortion of, the catalytic residues is apparent at 2.5 A resolution. A comparison of, prostaphopain B with the staphopain B-staphostatin B complex shows that, the proregion and the inhibitor interact with largely nonoverlapping parts, of the protease surface. In a modeled complex of prostaphopain B with, staphostatin B, clashes occur both inside and outside the active site, cleft, but involve mostly poorly ordered regions of the protein that may, be mobile.
About this Structure
1X9Y is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition., Filipek R, Szczepanowski R, Sabat A, Potempa J, Bochtler M, Biochemistry. 2004 Nov 9;43(44):14306-15. PMID:15518582
Page seeded by OCA on Wed Nov 21 05:55:39 2007
