1nlu

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(New page: 200px<br /><applet load="1nlu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nlu, resolution 1.30&Aring;" /> '''Pseudomonas sedolisi...)
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[[Image:1nlu.jpg|left|200px]]<br /><applet load="1nlu" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nlu.jpg|left|200px]]<br /><applet load="1nlu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nlu, resolution 1.30&Aring;" />
caption="1nlu, resolution 1.30&Aring;" />
'''Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin'''<br />
'''Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin'''<br />
==Overview==
==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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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==
==About this Structure==
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1NLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pseudomonalisin Pseudomonalisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.100 3.4.21.100] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NLU OCA].
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1NLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pseudomonalisin Pseudomonalisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.100 3.4.21.100] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLU OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
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[[Category: Dunn, B.M.]]
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[[Category: Dunn, B M.]]
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[[Category: Glodfarb, N.E.]]
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[[Category: Glodfarb, N E.]]
[[Category: Gustchina, A.]]
[[Category: Gustchina, A.]]
[[Category: Li, M.]]
[[Category: Li, M.]]
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[[Category: pscp]]
[[Category: pscp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:22:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:29 2008''

Revision as of 12:07, 21 February 2008

Image:1nlu.jpg

1nlu, resolution 1.30Å

Drag the structure with the mouse to rotate

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 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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