1f3u: Difference between revisions

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<StructureSection load='1f3u' size='340' side='right'caption='[[1f3u]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1f3u' size='340' side='right'caption='[[1f3u]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1f3u]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3U FirstGlance]. <br>
<table><tr><td colspan='2'>[[1f3u]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3U FirstGlance]. <br>
</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=1f3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3u OCA], [https://pdbe.org/1f3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3u RCSB], [https://www.ebi.ac.uk/pdbsum/1f3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3u ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=1f3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3u OCA], [https://pdbe.org/1f3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3u RCSB], [https://www.ebi.ac.uk/pdbsum/1f3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/T2FB_HUMAN T2FB_HUMAN]] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity.<ref>PMID:2477704</ref> [[https://www.uniprot.org/uniprot/T2FA_HUMAN T2FA_HUMAN]] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.<ref>PMID:10428810</ref> 
[https://www.uniprot.org/uniprot/T2FB_HUMAN T2FB_HUMAN] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity.<ref>PMID:2477704</ref>  
== 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=1f3u 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=1f3u ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
General transcription factor IIF (TFIIF) is required for transcription by RNA polymerase II; it consists minimally of a heterodimer of RNA polymerase-associated proteins RAP30 and RAP74. According to solution and mutagenesis studies, the multiple domains of RAP30 and RAP74 bind PolII, TFIIB, TAF250 and DNA in interactions that are essential for transcription initiation and elongation. The X-ray structure of the RAP30/RAP74 interaction domains at 1.7 A resolution reveals a novel "triple barrel" dimerization fold and suggests with mutant data that interactions with the transcription apparatus are mediated not only by this tripartite beta-barrel, but also via flexible loops and alpha and beta-structures extending from it.
Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution.,Gaiser F, Tan S, Richmond TJ J Mol Biol. 2000 Oct 6;302(5):1119-27. PMID:11183778<ref>PMID:11183778</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1f3u" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gaiser, F]]
[[Category: Gaiser F]]
[[Category: Richmond, T J]]
[[Category: Richmond TJ]]
[[Category: Tan, S]]
[[Category: Tan S]]
[[Category: Beta barrel]]
[[Category: General transcription initiation and elongation factor]]
[[Category: Novel dimerization fold]]
[[Category: Rna polymerase ii]]
[[Category: Transcription]]

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