1ga6: Difference between revisions

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[[Image:1ga6.gif|left|200px]]<br /><applet load="1ga6" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ga6.gif|left|200px]]
caption="1ga6, resolution 1.0&Aring;" />
 
'''CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)'''<br />
{{Structure
|PDB= 1ga6 |SIZE=350|CAPTION= <scene name='initialview01'>1ga6</scene>, resolution 1.0&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|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]
|GENE=
}}
 
'''CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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].  
1GA6 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=1GA6 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11323721 11323721]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11323721 11323721]
[[Category: Pseudomonalisin]]
[[Category: Pseudomonalisin]]
[[Category: Pseudomonas sp.]]
[[Category: Pseudomonas sp.]]
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[[Category: serine-carboxyl proteinase]]
[[Category: serine-carboxyl proteinase]]


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Revision as of 12:20, 20 March 2008

File:1ga6.gif


PDB ID 1ga6

Drag the structure with the mouse to rotate
, resolution 1.0Å
Ligands: , and
Activity: Pseudomonalisin, with EC number 3.4.21.100
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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 StructureAbout this Structure

1GA6 is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

ReferenceReference

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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