1gcb

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[[Image:1gcb.png|left|200px]]
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==GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)==
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<StructureSection load='1gcb' size='340' side='right' caption='[[1gcb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gcb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GCB FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1gcb RCSB], [http://www.ebi.ac.uk/pdbsum/1gcb PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gc/1gcb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 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.
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{{STRUCTURE_1gcb| PDB=1gcb | SCENE= }}
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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<ref>PMID:7638617</ref>
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===GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_7638617}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1gcb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCB OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:007638617</ref><ref group="xtra">PMID:015048824</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Johnston, S A.]]
[[Category: Johnston, S A.]]

Revision as of 10:51, 28 September 2014

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

1gcb, resolution 2.20Å

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