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[[Image:1j2x.jpg|left|200px]]
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{{STRUCTURE_1j2x|  PDB=1j2x  |  SCENE=  }}
'''Crystal structure of RAP74 C-terminal domain complexed with FCP1 C-terminal peptide'''


==Crystal structure of RAP74 C-terminal domain complexed with FCP1 C-terminal peptide==
<StructureSection load='1j2x' size='340' side='right'caption='[[1j2x]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1j2x]] is a 2 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=1J2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J2X FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=1j2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2x OCA], [https://pdbe.org/1j2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2x RCSB], [https://www.ebi.ac.uk/pdbsum/1j2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2x ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== 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/j2/1j2x_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=1j2x ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
After mRNA transcription termination in eukaryotes, the hyperphosphorylated form of RNA polymerase II (pol II0) must be recycled by TFIIF-associating C-terminal domain phosphatase (FCP1), the phosphatase responsible for dephosphorylating the C-terminal domain of the largest polymerase subunit. Transcription factor (TF)-IIF stimulates the activity of FCP1, and the RNA polymerase II-associating protein 74 subunit of TFIIF forms a complex with FCP1 in both human and yeast. Here, we report a cocrystal structure of the winged-helix domain of human RNA polymerase II-associating protein 74 bound to the alpha-helical C terminus of human FCP1 (residues 944-961). These results illustrate the molecular mechanism by which TFIIF efficiently recruits FCP1 to the pol II transcription machinery for recycling of the polymerase.


==Overview==
Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF.,Kamada K, Roeder RG, Burley SK Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2296-9. Epub 2003 Feb 18. PMID:12591941<ref>PMID:12591941</ref>
After mRNA transcription termination in eukaryotes, the hyperphosphorylated form of RNA polymerase II (pol II0) must be recycled by TFIIF-associating C-terminal domain phosphatase (FCP1), the phosphatase responsible for dephosphorylating the C-terminal domain of the largest polymerase subunit. Transcription factor (TF)-IIF stimulates the activity of FCP1, and the RNA polymerase II-associating protein 74 subunit of TFIIF forms a complex with FCP1 in both human and yeast. Here, we report a cocrystal structure of the winged-helix domain of human RNA polymerase II-associating protein 74 bound to the alpha-helical C terminus of human FCP1 (residues 944-961). These results illustrate the molecular mechanism by which TFIIF efficiently recruits FCP1 to the pol II transcription machinery for recycling of the polymerase.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1J2X is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2X OCA].
</div>
<div class="pdbe-citations 1j2x" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF., Kamada K, Roeder RG, Burley SK, Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2296-9. Epub 2003 Feb 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12591941 12591941]
*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Burley, S K.]]
[[Category: Burley SK]]
[[Category: Kamada, K.]]
[[Category: Kamada K]]
[[Category: Roeder, R G.]]
[[Category: Roeder RG]]
[[Category: Ctd]]
[[Category: Fcp1]]
[[Category: General transcription factor]]
[[Category: Phosphatase]]
[[Category: Rap30]]
[[Category: Rap74]]
[[Category: Rna polymerase ii]]
[[Category: Tfiif]]
[[Category: Winged-helix domain]]
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