1gcb
From Proteopedia
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|PDB= 1gcb |SIZE=350|CAPTION= <scene name='initialview01'>1gcb</scene>, resolution 2.2Å | |PDB= 1gcb |SIZE=350|CAPTION= <scene name='initialview01'>1gcb</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcb OCA], [http://www.ebi.ac.uk/pdbsum/1gcb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gcb RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Rees, D C.]] | [[Category: Rees, D C.]] | ||
[[Category: Xu, H E.]] | [[Category: Xu, H E.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: HG]] | ||
| - | [[Category: SO4]] | ||
[[Category: bleomycin hydrolase]] | [[Category: bleomycin hydrolase]] | ||
[[Category: cysteine protease]] | [[Category: cysteine protease]] | ||
| Line 36: | Line 36: | ||
[[Category: ring protein]] | [[Category: ring protein]] | ||
| - | ''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 20:41:16 2008'' |
Revision as of 17:41, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)
Overview
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.
About this Structure
1GCB is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6., Joshua-Tor L, Xu HE, Johnston SA, Rees DC, Science. 1995 Aug 18;269(5226):945-50. PMID:7638617
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