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==STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION==
==STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION==
<StructureSection load='1paa' size='340' side='right'caption='[[1paa]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1paa' size='340' side='right'caption='[[1paa]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1paa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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>
<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>
</td></tr><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<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>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ADR1_YEAST ADR1_YEAST]] Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).  
[https://www.uniprot.org/uniprot/ADR1_YEAST ADR1_YEAST] Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:8161501<ref>PMID:8161501</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1paa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bernstein, B E]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Herriott, J R]]
[[Category: Bernstein BE]]
[[Category: Hoffman, R C]]
[[Category: Herriott JR]]
[[Category: Horvath, S J]]
[[Category: Hoffman RC]]
[[Category: Klevit, R E]]
[[Category: Horvath SJ]]
[[Category: Transcription regulation]]
[[Category: Klevit RE]]

Latest revision as of 05:53, 17 April 2024

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

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