1nlu

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{{STRUCTURE_1nlu| PDB=1nlu | SCENE= }}
{{STRUCTURE_1nlu| PDB=1nlu | SCENE= }}
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'''Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin'''
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===Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin===
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==Overview==
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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).
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{{ABSTRACT_PUBMED_14733955}}
==About this Structure==
==About this Structure==
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[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: Pscp]]
[[Category: Pscp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:41:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:27:30 2008''

Revision as of 13:27, 29 July 2008

Template:STRUCTURE 1nlu

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

Template:ABSTRACT PUBMED 14733955

About this Structure

1NLU is a Single protein structure of sequence from Pseudomonas sp.. 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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