1a6r
From Proteopedia
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[[Category: self-compartmentalizing protease]] | [[Category: self-compartmentalizing protease]] | ||
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Revision as of 12:41, 30 October 2007
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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 SO4 as [ligand]. Structure known Active Sites: A73 and NUL. 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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