1A6R
GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A
Summary for 1A6R
| Entry DOI | 10.2210/pdb1a6r/pdb |
| Descriptor | GAL6, SULFATE ION (3 entities in total) |
| Functional Keywords | bleomycin hydrolase, peptidase, protease, dna-binding protein, self-compartmentalizing protease, hydrolase |
| 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 | 54629.83 |
| Authors | Joshua-Tor, L.,Zheng, W.,Johnston, S.A. (deposition date: 1998-02-27, release date: 1998-10-21, Last modification date: 2024-05-22) |
| Primary citation | Zheng, W.,Johnston, S.A.,Joshua-Tor, L. The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase. Cell(Cambridge,Mass.), 93:103-109, 1998 Cited by PubMed Abstract: The Gal6 protease is in a class of cysteine peptidases identified by their ability to inactivate the anti-cancer drug bleomycin. The protein forms a barrel structure with the active sites embedded in a channel as in the proteasome. In Gal6 the C termini lie in the active site clefts. We show that Gal6 acts as a carboxypeptidase on its C terminus to convert itself to an aminopeptidase and peptide ligase. The substrate specificity of the peptidase activity is determined by the position of the C terminus of Gal6 rather than the sequence of the substrate. We propose a model to explain these diverse activities and Gal6's singular ability to inactivate bleomycin. PubMed: 9546396DOI: 10.1016/S0092-8674(00)81150-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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