1a6r

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[[Image:1a6r.gif|left|200px]]
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{{STRUCTURE_1a6r| PDB=1a6r | SCENE= }}
{{STRUCTURE_1a6r| PDB=1a6r | SCENE= }}
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'''GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A'''
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===GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A===
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==Overview==
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The Gal6 protease is in a class of cysteine peptidases identified by their ability to inactivate the anti-cancer drug bleomycin. The protein forms a barrel structure with the active sites embedded in a channel as in the proteasome. In Gal6 the C termini lie in the active site clefts. We show that Gal6 acts as a carboxypeptidase on its C terminus to convert itself to an aminopeptidase and peptide ligase. The substrate specificity of the peptidase activity is determined by the position of the C terminus of Gal6 rather than the sequence of the substrate. We propose a model to explain these diverse activities and Gal6's singular ability to inactivate bleomycin.
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(as it appears on PubMed at http://www.pubmed.gov), where 9546396 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9546396}}
==About this Structure==
==About this Structure==
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[[Category: Protease]]
[[Category: Protease]]
[[Category: Self-compartmentalizing protease]]
[[Category: Self-compartmentalizing protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:53:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:15:46 2008''

Revision as of 13:15, 30 June 2008

Template:STRUCTURE 1a6r

GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A

Template:ABSTRACT PUBMED 9546396

About this Structure

1A6R is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase., Zheng W, Johnston SA, Joshua-Tor L, Cell. 1998 Apr 3;93(1):103-9. PMID:9546396

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