1a6r

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{{Seed}}
 
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[[Image:1a6r.png|left|200px]]
 
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==GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A==
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The line below this paragraph, containing "STRUCTURE_1a6r", creates the "Structure Box" on the page.
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<StructureSection load='1a6r' size='340' side='right'caption='[[1a6r]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1a6r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A6R FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1a6r| PDB=1a6r | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6r OCA], [https://pdbe.org/1a6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a6r RCSB], [https://www.ebi.ac.uk/pdbsum/1a6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6r ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLH1_YEAST BLH1_YEAST] The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.<ref>PMID:12555812</ref> <ref>PMID:16769724</ref>
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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/a6/1a6r_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/main_output.php?pdb_ID=1a6r 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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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.
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===GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A===
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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<ref>PMID:9546396</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_9546396}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1a6r" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 9546396 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9546396}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1A6R is a 1 chain structure of 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=1A6R OCA].
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==Reference==
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<ref group="xtra">PMID:9546396</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Johnston, S A.]]
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[[Category: Johnston SA]]
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[[Category: Joshua-Tor, L.]]
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[[Category: Joshua-Tor L]]
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[[Category: Zheng, W.]]
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[[Category: Zheng W]]
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[[Category: Bleomycin hydrolase]]
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[[Category: Dna-binding protein]]
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[[Category: Peptidase]]
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[[Category: Protease]]
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[[Category: Self-compartmentalizing protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 23:55:48 2009''
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Current revision

GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A

PDB ID 1a6r

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