1nlu

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spinqualitylabelsall models 1nlu, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin

Overview

High-resolution crystallographic analysis of a complex of the, serine-carboxyl proteinase sedolisin with pseudo-iodotyrostatin revealed, two molecules of this inhibitor bound in the active site of the enzyme, marking subsites from S3 to S3('). The mode of binding represents two, products of the proteolytic reaction. Substrate specificity of sedolisin, was investigated using peptide libraries and a new peptide substrate for, sedolisin, MCA-Lys-Pro-Pro-Leu-Glu#Tyr-Arg-Leu-Gly-Lys(DNP)-Gly, was, synthesized based on the results of the enzymatic and crystallographic, studies and was shown to be efficiently cleaved by the enzyme. The kinetic, parameters for the substrate, measured by the increase in fluorescence, upon relief of quenching, were: k(cat)=73+/-5 s(-1), K(m)=0.12+/-0.011, microM, and k(cat)/K(m)=608+/-85 s(-1)microM(-1).

About this Structure

1NLU is a Single protein structure of sequence from Pseudomonas sp. with CA as ligand. Active as Pseudomonalisin, with EC number 3.4.21.100 Full crystallographic information is available from OCA.

Reference

Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate., Wlodawer A, Li M, Gustchina A, Oyama H, Oda K, Beyer BB, Clemente J, Dunn BM, Biochem Biophys Res Commun. 2004 Feb 6;314(2):638-45. PMID:14733955

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