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==TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES== | |||
<StructureSection load='1tf3' size='340' side='right'caption='[[1tf3]]' scene=''> | |||
| | == Structural highlights == | ||
| | <table><tr><td colspan='2'>[[1tf3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TF3 FirstGlance]. <br> | ||
</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=1tf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tf3 OCA], [https://pdbe.org/1tf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tf3 RCSB], [https://www.ebi.ac.uk/pdbsum/1tf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tf3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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. | |||
== Evolutionary Conservation == | |||
== | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tf3_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1tf3 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three N-terminal zinc fingers of transcription factor IIIA bind in the DNA major groove. Substantial packing interfaces are formed between adjacent fingers, the linkers lose their intrinsic flexibility upon DNA binding, and several lysine side chains implicated in DNA recognition are dynamically disordered. | The three N-terminal zinc fingers of transcription factor IIIA bind in the DNA major groove. Substantial packing interfaces are formed between adjacent fingers, the linkers lose their intrinsic flexibility upon DNA binding, and several lysine side chains implicated in DNA recognition are dynamically disordered. | ||
Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA.,Foster MP, Wuttke DS, Radhakrishnan I, Case DA, Gottesfeld JM, Wright PE Nat Struct Biol. 1997 Aug;4(8):605-8. PMID:9253405<ref>PMID:9253405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1tf3" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Case | [[Category: Case DA]] | ||
[[Category: Foster | [[Category: Foster MP]] | ||
[[Category: Gottesfeld | [[Category: Gottesfeld JM]] | ||
[[Category: Radhakrishnan | [[Category: Radhakrishnan I]] | ||
[[Category: Wright | [[Category: Wright PE]] | ||
[[Category: Wuttke | [[Category: Wuttke DS]] | ||
Latest revision as of 12:12, 22 May 2024
TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURESTFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES
Structural highlights
FunctionTF3A_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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three N-terminal zinc fingers of transcription factor IIIA bind in the DNA major groove. Substantial packing interfaces are formed between adjacent fingers, the linkers lose their intrinsic flexibility upon DNA binding, and several lysine side chains implicated in DNA recognition are dynamically disordered. Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA.,Foster MP, Wuttke DS, Radhakrishnan I, Case DA, Gottesfeld JM, Wright PE Nat Struct Biol. 1997 Aug;4(8):605-8. PMID:9253405[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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