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1gat

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(New page: 200px<br /><applet load="1gat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gat" /> '''SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPL...)
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[[Image:1gat.gif|left|200px]]<br /><applet load="1gat" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gat" />
 
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'''SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPLEX OF THE ZINC CONTAINING DNA BINDING DOMAIN OF THE ERYTHROID TRANSCRIPTION FACTOR GATA-1 BY MULTIDIMENSIONAL NMR'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPLEX OF THE ZINC CONTAINING DNA BINDING DOMAIN OF THE ERYTHROID TRANSCRIPTION FACTOR GATA-1 BY MULTIDIMENSIONAL NMR==
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The high-resolution three-dimensional structure of a synthetic 57-residue, peptide comprising the double zinc finger of the human enhancer binding, protein MBP-1 has been determined in solution by nuclear magnetic, resonance spectroscopy on the basis of 1280 experimental restraints. A, total of 30 simulated annealing structures were calculated. The backbone, atomic root-mean-square distributions about the mean coordinate positions, are 0.32 and 0.33 A for the N- and C-terminal fingers, respectively, and, the corresponding values for all atoms, excluding disordered surface side, chains, are 0.36 and 0.40 A. Each finger comprises an irregular, antiparallel sheet and a helix, with the zinc tetrahedrally coordinated to, two cysteines and two histidines. The overall structure is nonglobular in, nature, and the angle between the long axes of the helices is 47 +/- 5, degrees. The long axis of the antiparallel sheet in the N-terminal finger, is approximately parallel to that of the helix in the C-terminal finger., Comparison of this structure with the X-ray structure of the Zif-268, triple finger complexed with DNA indicates that the relative orientation, of the individual zinc fingers is clearly distinct in the two cases. This, difference can be attributed to the presence of a long Lys side chain in, the C-terminal finger of MBP-1 at position 40, instead of a short Ala or, Ser side chain at the equivalent position in Zif-268. This finding, suggests that different contacts may be involved in the binding of the, zinc fingers of MBP-1 and Zif-268 to DNA, consistent with the findings, from methylation interference experiments that the two fingers of MBP-1, contact 10 base pairs, while the three fingers of Zif-268 contact only 9, base pairs.
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<StructureSection load='1gat' size='340' side='right'caption='[[1gat]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1gat]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GAT FirstGlance]. <br>
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1GAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] 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=1GAT 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=1gat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gat OCA], [https://pdbe.org/1gat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gat RCSB], [https://www.ebi.ac.uk/pdbsum/1gat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gat ProSAT]</span></td></tr>
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High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1., Omichinski JG, Clore GM, Robien M, Sakaguchi K, Appella E, Gronenborn AM, Biochemistry. 1992 Apr 28;31(16):3907-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1567844 1567844]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GATA1_CHICK GATA1_CHICK] Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.
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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/ga/1gat_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=1gat ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Clore, G.M.]]
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[[Category: Clore GM]]
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[[Category: Gronenborn, A.M.]]
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[[Category: Gronenborn AM]]
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[[Category: Omichinski, J.G.]]
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[[Category: Omichinski JG]]
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[[Category: ZN]]
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[[Category: dna]]
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[[Category: dna/transcription factor complex]]
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[[Category: double helix]]
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[[Category: nmr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:53:20 2007''
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Current revision

SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPLEX OF THE ZINC CONTAINING DNA BINDING DOMAIN OF THE ERYTHROID TRANSCRIPTION FACTOR GATA-1 BY MULTIDIMENSIONAL NMR

PDB ID 1gat

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