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2adr

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[[Image:2adr.gif|left|200px]]<br />
 
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<applet load="2adr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2adr" />
 
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'''ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES'''<br />
 
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==Overview==
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==ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES==
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The region responsible for sequence-specific DNA binding by the, transcription factor ADR1 contains two Cys2-His2 zinc fingers and an, additional N-terminal proximal accessory region (PAR). The N-terminal, (non-finger) PAR is unstructured in the absence of DNA and undergoes a, folding transition on binding the DNA transcription target site. We have, used a set of HN-HN NOEs derived from a perdeuterated protein-DNA complex, to describe the fold of ADR1 bound to the UAS1 binding site. The PAR forms, a compact domain consisting of three antiparallel strands that contact A-T, base pairs in the major groove. The three-strand domain is a novel fold, among all known DNA-binding proteins. The PAR shares sequence homology, with the N-terminal regions of other zinc finger proteins, suggesting that, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10331877 (full description)]]
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<StructureSection load='2adr' size='340' side='right'caption='[[2adr]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2adr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=2adr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adr OCA], [https://pdbe.org/2adr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2adr RCSB], [https://www.ebi.ac.uk/pdbsum/2adr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2adr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADR1_YEAST ADR1_YEAST] Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).
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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/ad/2adr_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=2adr 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 region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2-His2 zinc fingers and an additional N-terminal proximal accessory region (PAR). The N-terminal (non-finger) PAR is unstructured in the absence of DNA and undergoes a folding transition on binding the DNA transcription target site. We have used a set of HN-HN NOEs derived from a perdeuterated protein-DNA complex to describe the fold of ADR1 bound to the UAS1 binding site. The PAR forms a compact domain consisting of three antiparallel strands that contact A-T base pairs in the major groove. The three-strand domain is a novel fold among all known DNA-binding proteins. The PAR shares sequence homology with the N-terminal regions of other zinc finger proteins, suggesting that it represents a new DNA-binding module that extends the binding repertoire of zinc finger proteins.
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==About this Structure==
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A folding transition and novel zinc finger accessory domain in the transcription factor ADR1.,Bowers PM, Schaufler LE, Klevit RE Nat Struct Biol. 1999 May;6(5):478-85. PMID:10331877<ref>PMID:10331877</ref>
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2ADR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: ZNC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ADR OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A folding transition and novel zinc finger accessory domain in the transcription factor ADR1., Bowers PM, Schaufler LE, Klevit RE, Nat Struct Biol. 1999 May;6(5):478-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10331877 10331877]
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</div>
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<div class="pdbe-citations 2adr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Bowers PM]]
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[[Category: Bowers, P.M.]]
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[[Category: Kleivt RE]]
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[[Category: Kleivt, R.E.]]
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[[Category: ZN]]
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[[Category: adr1]]
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[[Category: nmr]]
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[[Category: transcription regulation]]
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[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:35:20 2007''
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Current revision

ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES

PDB ID 2adr

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