1go8

From Proteopedia

Revision as of 14:10, 5 November 2007

THE METZINCIN'S METHIONINE: PRTC M226L MUTANT

Overview

Serralysins are a family of metalloproteases secreted by Gram-negative, bacteria into the medium in the form of inactive zymogens. Usually, all, serralysin secretors have on the same operon a gene coding for a, periplasmic 10-kDa protein, which is an inhibitor of the secreted, protease. The recent characterization of the inhibitor of the alkaline, protease from Pseudomonas aeruginosa revealed a surprisingly low, dissociation constant of 4 pm, contrary to earlier studies on homologous, systems, where inhibition constants in the microm range were reported. To, approach a more accurate understanding, the crystal structure of the, complex between inhibitor and protease from P. aeruginosa was determined, at 1.74 A resolution and refined to R(free) = 0.204. The structure, reported here shows clearly that the N terminus of the inhibitor forms a, coordinative bond to the catalytic Zn(2+) ion with a nitrogen-zinc, distance of 2.17 A. We conclude that this interaction adds substantially, to the complex stability and show also that similar interactions are found, in other metzincin-inhibitor complexes.

About this Structure

1GO8 is a Single protein structure of sequence from Erwinia chrysanthemi with CA, ZN and PO4 as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond., Hege T, Feltzer RE, Gray RD, Baumann U, J Biol Chem. 2001 Sep 14;276(37):35087-92. Epub 2001 Jul 9. PMID:11445573

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