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2k7l

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NMR structure of a complex formed by the C-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1

Structural highlights

2k7l is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	GTF2F1, RAP74 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

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 PubMed

Recycling of RNA polymerase II (RNAPII) requires dephosphorylation of the C-terminal domain (CTD) of the largest subunit of the polymerase. FCP1 enables the recycling of RNAPII via its CTD-specific phosphatase activity, which is stimulated by the RAP74 subunit of the general transcription factor TFIIF. Both the central (centFCP1) and C-terminal (cterFCP1) domains of FCP1 interact independently and specifically with the C-terminal domain of RAP74 (cterRAP74), suggesting that these interactions mediate the stimulatory effect of TFIIF on the CTD phosphatase activity of FCP1. Phosphorylation of FCP1 by casein kinase 2 on residues in its central (T584) and C-terminal (S942 and S944) domains stimulates its binding to RAP74 and its CTD phosphatase activity. To improve our understanding of the FCP1-RAP74 interactions, we previously determined the NMR structure of a complex formed by human cterRAP74 and cterFCP1. We now present the high-resolution NMR structure and thermodynamic characterization by isothermal titration calorimetry of a complex formed by the same cterRAP74 domain and a phosphorylated peptide from the central domain of human FCP1 (centFCP1-PO(4)). Comparison of the cterFCP1-cterRAP74 and centFCP1-PO(4)-cterRAP74 complexes indicates that centFCP1 and cterFCP1 both utilize hydrophobic and acidic residues to recognize the same groove of RAP74, but there are significant differences in the details of their interactions. These differences point to the adaptability of RAP74 to recognize the two regions of FCP1. Our NMR and thermodynamic studies further elucidate the complex molecular mechanism by which TFIIF and FCP1 cooperate for RNAPII recycling.

NMR structure of a complex formed by the carboxyl-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1 phosphatase.,Yang A, Abbott KL, Desjardins A, Di Lello P, Omichinski JG, Legault P Biochemistry. 2009 Mar 10;48(9):1964-74. PMID:19215094^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rossignol M, Keriel A, Staub A, Egly JM. Kinase activity and phosphorylation of the largest subunit of TFIIF transcription factor. J Biol Chem. 1999 Aug 6;274(32):22387-92. PMID:10428810
↑ Yang A, Abbott KL, Desjardins A, Di Lello P, Omichinski JG, Legault P. NMR structure of a complex formed by the carboxyl-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1 phosphatase. Biochemistry. 2009 Mar 10;48(9):1964-74. PMID:19215094 doi:10.1021/bi801549m

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k7l"

@@ Line 1: / Line 1: @@
 ==NMR structure of a complex formed by the C-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1==
-<StructureSection load='2k7l' size='340' side='right' caption='[[2k7l]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
+<StructureSection load='2k7l' size='340' side='right'caption='[[2k7l]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2k7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K7L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2k7l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K7L FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GTF2F1, RAP74 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GTF2F1, RAP74 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7l OCA], [http://pdbe.org/2k7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k7l RCSB], [http://www.ebi.ac.uk/pdbsum/2k7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7l ProSAT]</span></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=2k7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7l OCA], [https://pdbe.org/2k7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7l RCSB], [https://www.ebi.ac.uk/pdbsum/2k7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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/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]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Transcription initiation factor|Transcription initiation factor]]
+*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
 == References ==
 <references/>
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Abbott, K L]]
 [[Category: Desjardins, A]]

2k7l

From Proteopedia

Current revision

NMR structure of a complex formed by the C-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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