1a6r

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==Overview==
==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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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.
==About this Structure==
==About this Structure==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Johnston, S.A.]]
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[[Category: Johnston, S A.]]
[[Category: Joshua-Tor, L.]]
[[Category: Joshua-Tor, L.]]
[[Category: Zheng, W.]]
[[Category: Zheng, W.]]
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[[Category: self-compartmentalizing protease]]
[[Category: self-compartmentalizing protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:29:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:27 2008''

Revision as of 09:41, 21 February 2008


1a6r, resolution 2.05Å

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GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A

Overview

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.

About this Structure

1A6R is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Known structural/functional Sites: and . 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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