1go7
From Proteopedia
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THE METZINCIN'S METHIONINE: PRTC M226C-E189K DOUBLE 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
1GO7 is a Single protein structure of sequence from Erwinia chrysanthemi with , and as ligands. Known structural/functional Site: . 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
Page seeded by OCA on Sun Feb 3 09:41:21 2008
Categories: Erwinia chrysanthemi | Single protein | Hege, T. | CA | PO4 | ZN | Hydrolase | Metalloprotease | Protease
