Joshua-Tor, L., Xu, H., Johnston, S., Rees, D. (August 1995) Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6. Science, 269 (5226). pp. 945-950. ISSN 0036-80751095-9203 (Public Dataset)
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: | 18 August 1995 |
| Date Deposited: | 07 Dec 2015 16:32 |
| Last Modified: | 06 Sep 2017 15:47 |
| Related URLs: | |
| Dataset ID: | |
| URI: | https://repository.cshl.edu/id/eprint/32017 |
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