1nlu

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[[Image:1nlu.jpg|left|200px]]<br /><applet load="1nlu" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nlu.jpg|left|200px]]
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caption="1nlu, resolution 1.30&Aring;" />
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'''Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin'''<br />
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{{Structure
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|PDB= 1nlu |SIZE=350|CAPTION= <scene name='initialview01'>1nlu</scene>, resolution 1.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [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]
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|GENE= PCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Pseudomonas sp.])
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}}
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'''Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin'''
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==Overview==
==Overview==
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==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 <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].
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1NLU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLU OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14733955 14733955]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14733955 14733955]
[[Category: Pseudomonalisin]]
[[Category: Pseudomonalisin]]
[[Category: Pseudomonas sp.]]
[[Category: Pseudomonas sp.]]
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[[Category: pscp]]
[[Category: pscp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:30 2008''

Revision as of 10:58, 20 March 2008

Image:1nlu.jpg


PDB ID 1nlu

Drag the structure with the mouse to rotate
, resolution 1.30Å
Ligands:
Gene: PCP (Pseudomonas sp.)
Activity: Pseudomonalisin, with EC number 3.4.21.100
Coordinates: save as pdb, mmCIF, xml



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.. 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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