1ga6

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(New page: 200px<br /><applet load="1ga6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ga6, resolution 1.0&Aring;" /> '''CRYSTAL STRUCTURE ANA...)
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'''CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)'''<br />
'''CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)'''<br />
==Overview==
==Overview==
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The crystal structure of a pepstatin-insensitive carboxyl proteinase from, Pseudomonas sp. 101 (PSCP) has been solved by single-wavelength anomalous, diffraction using the absorption peak of bromide anions. Structures of the, uninhibited enzyme and of complexes with an inhibitor that was either, covalently or noncovalently bound were refined at 1.0-1.4 A resolution., The structure of PSCP comprises a single compact domain with a diameter of, approximately 55 A, consisting of a seven-stranded parallel beta-sheet, flanked on both sides by a number of helices. The fold of PSCP is a, superset of the subtilisin fold, and the covalently bound inhibitor is, linked to the enzyme through a serine residue. Thus, the structure of PSCP, defines a novel family of serine-carboxyl proteinases (defined as MEROPS, S53) with a unique catalytic triad consisting of Glu 80, Asp 84 and Ser, 287.
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The crystal structure of a pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. 101 (PSCP) has been solved by single-wavelength anomalous diffraction using the absorption peak of bromide anions. Structures of the uninhibited enzyme and of complexes with an inhibitor that was either covalently or noncovalently bound were refined at 1.0-1.4 A resolution. The structure of PSCP comprises a single compact domain with a diameter of approximately 55 A, consisting of a seven-stranded parallel beta-sheet flanked on both sides by a number of helices. The fold of PSCP is a superset of the subtilisin fold, and the covalently bound inhibitor is linked to the enzyme through a serine residue. Thus, the structure of PSCP defines a novel family of serine-carboxyl proteinases (defined as MEROPS S53) with a unique catalytic triad consisting of Glu 80, Asp 84 and Ser 287.
==About this Structure==
==About this Structure==
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1GA6 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, ACT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1GA6 OCA].
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1GA6 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>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1GA6 OCA].
==Reference==
==Reference==
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[[Category: serine-carboxyl proteinase]]
[[Category: serine-carboxyl proteinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:52:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:53 2008''

Revision as of 10:47, 21 February 2008

Image:1ga6.gif

1ga6, resolution 1.0Å

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CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)

Overview

The crystal structure of a pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. 101 (PSCP) has been solved by single-wavelength anomalous diffraction using the absorption peak of bromide anions. Structures of the uninhibited enzyme and of complexes with an inhibitor that was either covalently or noncovalently bound were refined at 1.0-1.4 A resolution. The structure of PSCP comprises a single compact domain with a diameter of approximately 55 A, consisting of a seven-stranded parallel beta-sheet flanked on both sides by a number of helices. The fold of PSCP is a superset of the subtilisin fold, and the covalently bound inhibitor is linked to the enzyme through a serine residue. Thus, the structure of PSCP defines a novel family of serine-carboxyl proteinases (defined as MEROPS S53) with a unique catalytic triad consisting of Glu 80, Asp 84 and Ser 287.

About this Structure

1GA6 is a Single protein structure of sequence from Pseudomonas sp. with , and as ligands. Active as Pseudomonalisin, with EC number 3.4.21.100 Full crystallographic information is available from OCA.

Reference

Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes., Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K, Nat Struct Biol. 2001 May;8(5):442-6. PMID:11323721

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