1gcb
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(New page: 200px<br /><applet load="1gcb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gcb, resolution 2.2Å" /> '''GAL6, YEAST BLEOMYCIN...)
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Revision as of 13:48, 20 November 2007
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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 with SO4, HG and GOL as ligands. 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 Tue Nov 20 15:56:06 2007
