1un6

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[[Image:1un6.jpg|left|200px]]<br /><applet load="1un6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1un6, resolution 3.10&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF A ZINC FINGER- RNA COMPLEX REVEALS TWO MODES OF MOLECULAR RECOGNITION'''<br />
 
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==Overview==
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==THE CRYSTAL STRUCTURE OF A ZINC FINGER - RNA COMPLEX REVEALS TWO MODES OF MOLECULAR RECOGNITION==
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Zinc-finger proteins of the classical Cys2His2 type are the most, frequently used class of transcription factor and account for about 3% of, genes in the human genome. The zinc-finger motif was discovered during, biochemical studies on the transcription factor TFIIIA, which regulates, the 5S ribosomal RNA genes of Xenopus laevis. Zinc-fingers mostly interact, with DNA, but TFIIIA binds not only specifically to the promoter DNA, but, also to 5S RNA itself. Increasing evidence indicates that zinc-fingers are, more widely used to recognize RNA. There have been numerous structural, studies on DNA binding, but none on RNA binding by zinc-finger proteins., Here we report the crystal structure of a three-finger complex with 61, bases of RNA, derived from the central regions of the complete nine-finger, TFIIIA-5S RNA complex. The structure reveals two modes of zinc-finger, binding, both of which differ from that in common use for DNA: first, the, zinc-fingers interact with the backbone of a double helix; and second, the, zinc-fingers specifically recognize individual bases positioned for access, in otherwise intricately folded 'loop' regions of the RNA.
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<StructureSection load='1un6' size='340' side='right'caption='[[1un6]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1un6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The March 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Zinc Fingers'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_3 10.2210/rcsb_pdb/mom_2007_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UN6 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">X-ray diffraction, [[Resolution|Resolution]] 3.1&#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=MG:MAGNESIUM+ION'>MG</scene>, <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=1un6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un6 OCA], [https://pdbe.org/1un6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1un6 RCSB], [https://www.ebi.ac.uk/pdbsum/1un6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1un6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TF3A_XENLA TF3A_XENLA] Acts as both a positive transcription factor for 5S RNA genes and a specific RNA binding protein that complexes with 5S RNA in oocytes to form the 7S ribonucleoprotein storage particle. May play an essential role in the developmental change in 5S RNA gene expression. Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III. Also binds the transcribed 5S RNA's.
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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/un/1un6_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=1un6 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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Zinc-finger proteins of the classical Cys2His2 type are the most frequently used class of transcription factor and account for about 3% of genes in the human genome. The zinc-finger motif was discovered during biochemical studies on the transcription factor TFIIIA, which regulates the 5S ribosomal RNA genes of Xenopus laevis. Zinc-fingers mostly interact with DNA, but TFIIIA binds not only specifically to the promoter DNA, but also to 5S RNA itself. Increasing evidence indicates that zinc-fingers are more widely used to recognize RNA. There have been numerous structural studies on DNA binding, but none on RNA binding by zinc-finger proteins. Here we report the crystal structure of a three-finger complex with 61 bases of RNA, derived from the central regions of the complete nine-finger TFIIIA-5S RNA complex. The structure reveals two modes of zinc-finger binding, both of which differ from that in common use for DNA: first, the zinc-fingers interact with the backbone of a double helix; and second, the zinc-fingers specifically recognize individual bases positioned for access in otherwise intricately folded 'loop' regions of the RNA.
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==About this Structure==
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Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition.,Lu D, Searles MA, Klug A Nature. 2003 Nov 6;426(6962):96-100. PMID:14603324<ref>PMID:14603324</ref>
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1UN6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with ZN and MG as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1UN6 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb87_1.html Zinc Fingers]]. Known structural/functional Site: <scene name='pdbsite=BN4:Zn-Binding Site'>BN4</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UN6 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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Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition., Lu D, Searles MA, Klug A, Nature. 2003 Nov 6;426(6962):96-100. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14603324 14603324]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1un6" 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]]
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[[Category: RCSB PDB Molecule of the Month]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Zinc Fingers]]
[[Category: Zinc Fingers]]
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[[Category: Klug, A.]]
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[[Category: Klug A]]
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[[Category: Lu, D.]]
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[[Category: Lu D]]
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[[Category: Searles, M.A.]]
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[[Category: Searles MA]]
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[[Category: MG]]
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[[Category: ZN]]
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[[Category: 5s ribosomal rna]]
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[[Category: dna-binding]]
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[[Category: nuclear protein]]
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[[Category: rna-binding]]
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[[Category: rna-protein complex]]
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[[Category: tfiiia]]
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[[Category: transcription regulation]]
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[[Category: x. laevis]]
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[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:03:58 2007''
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Current revision

THE CRYSTAL STRUCTURE OF A ZINC FINGER - RNA COMPLEX REVEALS TWO MODES OF MOLECULAR RECOGNITION

PDB ID 1un6

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