Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6

Joshua-Tor, L., Xu, H., Johnston, S., Rees, D. (1995) Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6. Science, 269 (5226). pp. 945-950. ISSN 0036-80751095-9203

URL: http://www.ncbi.nlm.nih.gov/pubmed/7638617
DOI: 10.1126/science.7638617

Abstract

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 Angstrom 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.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > bleomycin hydrolase
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Joshua-Tor lab
Depositing User: Matt Covey
Date Deposited: 07 Dec 2015 16:32
Last Modified: 06 Sep 2017 15:47
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Dataset ID:
URI: http://repository.cshl.edu/id/eprint/32017

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