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1a6r
From Proteopedia
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|PDB= 1a6r |SIZE=350|CAPTION= <scene name='initialview01'>1a6r</scene>, resolution 2.05Å | |PDB= 1a6r |SIZE=350|CAPTION= <scene name='initialview01'>1a6r</scene>, resolution 2.05Å | ||
|SITE= <scene name='pdbsite=A73:Nucleophilic+CYS+Mutated+To+ALA'>A73</scene> and <scene name='pdbsite=NUL:Catalytic+Residues'>NUL</scene> | |SITE= <scene name='pdbsite=A73:Nucleophilic+CYS+Mutated+To+ALA'>A73</scene> and <scene name='pdbsite=NUL:Catalytic+Residues'>NUL</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= GAL6C73A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= GAL6C73A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6r OCA], [http://www.ebi.ac.uk/pdbsum/1a6r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a6r RCSB]</span> | ||
}} | }} | ||
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[[Category: Joshua-Tor, L.]] | [[Category: Joshua-Tor, L.]] | ||
[[Category: Zheng, W.]] | [[Category: Zheng, W.]] | ||
| - | [[Category: SO4]] | ||
[[Category: bleomycin hydrolase]] | [[Category: bleomycin hydrolase]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
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[[Category: self-compartmentalizing protease]] | [[Category: self-compartmentalizing protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:26 2008'' |
Revision as of 15:34, 30 March 2008
| |||||||
| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Gene: | GAL6C73A (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A
Overview
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.
About this Structure
1A6R is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase., Zheng W, Johnston SA, Joshua-Tor L, Cell. 1998 Apr 3;93(1):103-9. PMID:9546396
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