1a6r
From Proteopedia
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. 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 Page seeded by OCA on Fri May 2 09:53:59 2008
