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'''GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)''' | '''GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)''' | ||
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[[Category: Rees, D C.]] | [[Category: Rees, D C.]] | ||
[[Category: Xu, H E.]] | [[Category: Xu, H E.]] | ||
[[Category: | [[Category: Bleomycin hydrolase]] | ||
[[Category: | [[Category: Cysteine protease]] | ||
[[Category: | [[Category: Dna-binding]] | ||
[[Category: | [[Category: Peptidase]] | ||
[[Category: | [[Category: Regulatory factor]] | ||
[[Category: | [[Category: Ring protein]] | ||
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Revision as of 14:24, 2 May 2008
GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)
Overview
Bleomycin hydrolase is a cysteine protease that hydrolyzes the anticancer drug bleomycin. The homolog in yeast, Gal6, has recently been identified and found to bind DNA and to act as a repressor in the Gal4 regulatory system. The crystal structure of Gal6 at 2.2 A resolution reveals a hexameric structure with a prominent central channel. The papain-like active sites are situated within the central channel, in a manner resembling the organization of active sites in the proteasome. The Gal6 channel is lined with 60 lysine residues from the six subunits, suggesting a role in DNA binding. The carboxyl-terminal arm of Gal6 extends into the active site cleft and may serve a regulatory function. Rather than each residing in distinct, separable domains, the protease and DNA-binding activities appear structurally intertwined in the hexamer, implying a coupling of these two activities.
About this Structure
1GCB is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6., Joshua-Tor L, Xu HE, Johnston SA, Rees DC, Science. 1995 Aug 18;269(5226):945-50. PMID:7638617 Page seeded by OCA on Fri May 2 17:24:32 2008
