1GCB

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

Summary for 1GCB

• Entry DOI: 10.2210/pdb1gcb/pdb
• Descriptor: GAL6 HG (EMTS) DERIVATIVE, SULFATE ION, MERCURY (II) ION, ... (5 entities in total)
• Functional Keywords: dna-binding, peptidase, cysteine protease, regulatory factor, bleomycin hydrolase, ring protein, dna-binding protein, dna binding protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Isoform Cytoplasmic: Cytoplasm. Isoform Mitochondrial: Mitochondrion: Q01532
• Total number of polymer chains: 1
• Total formula weight: 53335.04

Authors

Joshua-Tor, L.,Xu, H.E.,Johnston, S.A.,Rees, D.C. (deposition date: 1995-07-18, release date: 1995-10-15, Last modification date: 2024-02-07)

Primary citation

Joshua-Tor, L.,Xu, H.E.,Johnston, S.A.,Rees, D.C.
Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6.
Science, 269:945-950, 1995

PubMed 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 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.

PubMed: 7638617

Experimental method

X-RAY DIFFRACTION (2.2 Å)