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

Joshua-Tor, Leemor and Xu, H. Eric and Johnston, Stephen Albert and Rees, Douglas C. (1995) Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6. Science, 269 (5226). pp. 945-950. ISSN 0036-8075. doi:10.1126/science.7638617.

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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 Å 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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Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 1995 American Association for the Advancement of Science. Received 3 March 1995; accepted 7 July 1995. We thank M. Stowell for help in synchrotron data collection; W. Zheng for discussions and unpublished results; members of the Stanford Synchrotron Radiation Laboratory (SSRL) and the Cornell High Energy Synchrotron Source (CHESS) for assistance during data collection; A. Wu for the sedimentation experiments and mass spectometry; K. Swiderek for sequencing; R. Huber for coordinates of human cathepsin B, and W. Saenger and R. Hilgenfeld for coordinates of calotropin. Supported in part by the Caltech Consortium in Chemistry and Chemical Engineering (L.J. and D.C.R.), grants from NIH (GM40700) and Human Frontier Science Program (S.A.J.), and by a postdoctoral fellowship from the Jane Coffin Childs Memorial Fund for Medical Research (L.J.). The diffraction facility was supported in part by USPHS grant GM45162 and the Beckman Institute (D.C.R.), and the Howard Hughes Medical Institute (to P. J. Bjorkman). The rotation camera facility at the Stanford Synchrotron Radiation Laboratory is supported by the Department of Energy, Office of Basic Energy Sciences and the National Institutes of Health Biomedical Research Technology Program, Division of Research Resources. X-PLOR calculations were done on the CRAY C90 at the San Diego Supercomputer Center, supported by the NSF. Coordinates have been deposited in the Brookhaven Data Bank (IGCB) and are available by e-mail (
Funding AgencyGrant Number
Caltech Consortium in Chemistry and Chemical EngineeringUNSPECIFIED
Human Frontier Science ProgramUNSPECIFIED
Jane Coffin Childs Memorial Fund for Medical ResearchUNSPECIFIED
Caltech Beckman InstituteUNSPECIFIED
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Department of Energy (DOE)UNSPECIFIED
Issue or Number:5226
Record Number:CaltechAUTHORS:20141208-090927193
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Official Citation:Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6 L Joshua-Tor, HE Xu, SA Johnston, and DC Rees Science 18 August 1995: 269 (5226), 945-950. [DOI:10.1126/science.7638617]
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52455
Deposited By: Tony Diaz
Deposited On:09 Dec 2014 22:21
Last Modified:10 Nov 2021 19:41

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