1tba

From Proteopedia

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Revision as of 09:24, 29 September 2021

SOLUTION STRUCTURE OF A TBP-TAFII230 COMPLEX: PROTEIN MIMICRY OF THE MINOR GROOVE SURFACE OF THE TATA BOX UNWOUND BY TBP, NMR, 25 STRUCTURES

Structural highlights

1tba is a 2 chain structure with sequence from Atcc 18824 and Drome. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TAF1_DROME] TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Largest component and core scaffold of the complex. Contains N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. The C-terminal Ser/Thr kinase domain phosphorylates histone H2B at 'Ser-33', which may contribute to transcriptional activation during embryogenesis. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Negative regulator of the TATA box-binding activity of Tbp.^[1] ^[2] ^[3] ^[4] [TBP_YEAST] General transcription factor that functions at the core of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.^[5] ^[6] ^[7]

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

General transcription factor TFIID consists of TATA box-binding protein (TBP) and TBP-associated factors (TAF(II)s), which together play a central role in both positive and negative regulation of transcription. The N-terminal region of the 230 kDa Drosophila TAF(II) (dTAF(II)230) binds directly to TBP and inhibits TBP binding to the TATA box. We report here the solution structure of the complex formed by dTAF(II)230 N-terminal region (residues 11-77) and TBP. dTAF(II)230(11-77) comprises three alpha helices and a beta hairpin, forming a core that occupies the concave DNA-binding surface of TBP. The TBP-binding surface of dTAF(II)230 markedly resembles the minor groove surface of the partially unwound TATA box in the TBP-TATA complex. This protein mimicry of the TATA element surface provides the structural basis of the mechanism by which dTAF(II)230 negatively controls the TATA box-binding activity within the TFIID complex.

Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP.,Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M Cell. 1998 Sep 4;94(5):573-83. PMID:9741622^[8]

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

References

↑ Kokubo T, Gong DW, Yamashita S, Horikoshi M, Roeder RG, Nakatani Y. Drosophila 230-kD TFIID subunit, a functional homolog of the human cell cycle gene product, negatively regulates DNA binding of the TATA box-binding subunit of TFIID. Genes Dev. 1993 Jun;7(6):1033-46. PMID:8504928
↑ Dikstein R, Ruppert S, Tjian R. TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74. Cell. 1996 Mar 8;84(5):781-90. PMID:8625415
↑ Maile T, Kwoczynski S, Katzenberger RJ, Wassarman DA, Sauer F. TAF1 activates transcription by phosphorylation of serine 33 in histone H2B. Science. 2004 May 14;304(5673):1010-4. PMID:15143281 doi:http://dx.doi.org/10.1126/science.1095001
↑ Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M. Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. Cell. 1998 Sep 4;94(5):573-83. PMID:9741622
↑ Hampsey M. Molecular genetics of the RNA polymerase II general transcriptional machinery. Microbiol Mol Biol Rev. 1998 Jun;62(2):465-503. PMID:9618449
↑ Sanders SL, Garbett KA, Weil PA. Molecular characterization of Saccharomyces cerevisiae TFIID. Mol Cell Biol. 2002 Aug;22(16):6000-13. PMID:12138208
↑ Martinez E. Multi-protein complexes in eukaryotic gene transcription. Plant Mol Biol. 2002 Dec;50(6):925-47. PMID:12516863
↑ Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M. Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. Cell. 1998 Sep 4;94(5):573-83. PMID:9741622

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/1tba"

@@ Line 3: / Line 3: @@
 <StructureSection load='1tba' size='340' side='right'caption='[[1tba]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tba]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TBA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tba]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [https://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TBA FirstGlance]. <br>
-</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=1tba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tba OCA], [http://pdbe.org/1tba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tba RCSB], [http://www.ebi.ac.uk/pdbsum/1tba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tba ProSAT]</span></td></tr>
+</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=1tba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tba OCA], [https://pdbe.org/1tba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tba RCSB], [https://www.ebi.ac.uk/pdbsum/1tba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tba ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TAF1_DROME TAF1_DROME]] TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Largest component and core scaffold of the complex. Contains N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. The C-terminal Ser/Thr kinase domain phosphorylates histone H2B at 'Ser-33', which may contribute to transcriptional activation during embryogenesis. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Negative regulator of the TATA box-binding activity of Tbp.<ref>PMID:8504928</ref> <ref>PMID:8625415</ref> <ref>PMID:15143281</ref> <ref>PMID:9741622</ref>  [[http://www.uniprot.org/uniprot/TBP_YEAST TBP_YEAST]] General transcription factor that functions at the core of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.<ref>PMID:9618449</ref> <ref>PMID:12138208</ref> <ref>PMID:12516863</ref>
+[[https://www.uniprot.org/uniprot/TAF1_DROME TAF1_DROME]] TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Largest component and core scaffold of the complex. Contains N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. The C-terminal Ser/Thr kinase domain phosphorylates histone H2B at 'Ser-33', which may contribute to transcriptional activation during embryogenesis. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Negative regulator of the TATA box-binding activity of Tbp.<ref>PMID:8504928</ref> <ref>PMID:8625415</ref> <ref>PMID:15143281</ref> <ref>PMID:9741622</ref>  [[https://www.uniprot.org/uniprot/TBP_YEAST TBP_YEAST]] General transcription factor that functions at the core of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.<ref>PMID:9618449</ref> <ref>PMID:12138208</ref> <ref>PMID:12516863</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
 *[[Heat Shock Protein structures|Heat Shock Protein structures]]
-*[[TATA-Binding Protein|TATA-Binding Protein]]
+*[[TATA-binding protein 3D structures|TATA-binding protein 3D structures]]
-*[[Transcription initiation factor|Transcription initiation factor]]
+*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
 == References ==
 <references/>

1tba

From Proteopedia

Revision as of 09:24, 29 September 2021

SOLUTION STRUCTURE OF A TBP-TAFII230 COMPLEX: PROTEIN MIMICRY OF THE MINOR GROOVE SURFACE OF THE TATA BOX UNWOUND BY TBP, NMR, 25 STRUCTURES

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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