1paa

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(New page: 200px<br /><applet load="1paa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1paa" /> '''STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC F...)
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[[Image:1paa.gif|left|200px]]<br /><applet load="1paa" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1paa" />
 
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'''STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION'''<br />
 
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==Overview==
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==STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION==
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The solution structure for a mutant zinc finger peptide based on the, sequence of the C-terminal ADR1 finger has been determined by, two-dimensional NMR spectroscopy. The mutant peptide, called PAPA, has, both proline residues from the wild-type sequence replaced with alanines., A nonessential cysteine was also replaced with alanine. The behavior of, PAPA in solution implicates the prolines in the conformational, heterogeneity reported earlier for the wild-type peptide [Xu, R. X., Horvath, S. J., &amp; Klevit, R. E. (1991) Biochemistry 30, 3365-3371]. The, solution structure of PAPA reveals several interesting features of the, zinc finger motif. The residue immediately following the second cysteine, ligand adopts a positive phi angle, which we propose is a common feature, of this class of zinc fingers, regardless of whether this residue is a, glycine. The NMR spectrum and resulting solution structure of PAPA suggest, that a side-chain to side-chain hydrogen bond involving an arginine and an, aspartic acid analogous to one observed in the Zif268 protein-DNA, cocrystal structure exists in solution in the absence of DNA [Pavletich, N. P., &amp; Pabo, C. O. (1991) Science 252, 809-817]. A model for the, interaction between the two ADR1 zinc fingers and their DNA binding sites, was built by superpositioning the refined solution structures of PAPA and, ADR1b onto the Zif268 structure. This model offers structural explanations, for a variety of mutations to the ADR1 zinc finger domains that have been, shown to affect DNA-binding affinity or specificity.
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<StructureSection load='1paa' size='340' side='right'caption='[[1paa]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1paa]] 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=1PAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PAA FirstGlance]. <br>
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1PAA 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]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PAA OCA].
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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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==Reference==
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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=1paa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1paa OCA], [https://pdbe.org/1paa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1paa RCSB], [https://www.ebi.ac.uk/pdbsum/1paa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1paa ProSAT]</span></td></tr>
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Structure of a histidine-X4-histidine zinc finger domain: insights into ADR1-UAS1 protein-DNA recognition., Bernstein BE, Hoffman RC, Horvath S, Herriott JR, Klevit RE, Biochemistry. 1994 Apr 19;33(15):4460-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8161501 8161501]
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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/pa/1paa_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=1paa ConSurf].
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<div style="clear:both"></div>
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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: Bernstein BE]]
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[[Category: Bernstein, B.E.]]
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[[Category: Herriott JR]]
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[[Category: Herriott, J.R.]]
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[[Category: Hoffman RC]]
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[[Category: Hoffman, R.C.]]
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[[Category: Horvath SJ]]
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[[Category: Horvath, S.J.]]
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[[Category: Klevit RE]]
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[[Category: Klevit, R.E.]]
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[[Category: ZN]]
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[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:37:58 2007''
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Current revision

STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION

PDB ID 1paa

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