1gcb: Difference between revisions

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[[Image:1gcb.jpg|left|200px]]
{{Seed}}
[[Image:1gcb.png|left|200px]]


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{{STRUCTURE_1gcb|  PDB=1gcb  |  SCENE=  }}  
{{STRUCTURE_1gcb|  PDB=1gcb  |  SCENE=  }}  


'''GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)'''
===GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)===




==Overview==
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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.
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{{ABSTRACT_PUBMED_7638617}}


==About this Structure==
==About this Structure==
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[[Category: Regulatory factor]]
[[Category: Regulatory factor]]
[[Category: Ring protein]]
[[Category: Ring protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:24:32 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:04:21 2008''

Revision as of 02:04, 1 July 2008

File:1gcb.png

Template:STRUCTURE 1gcb

GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)

Template:ABSTRACT PUBMED 7638617

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

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