5M4S

Transcription factor TFIIA as a single chain protein

Summary for 5M4S

• Entry DOI: 10.2210/pdb5m4s/pdb
• Descriptor: Transcription initiation factor IIA subunit 2,Transcription initiation factor IIA subunit 1,Transcription initiation factor IIA subunit 1 (2 entities in total)
• Functional Keywords: tfiid, tfiia, transcription, single chain
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus: P52655
• Total number of polymer chains: 1
• Total formula weight: 24134.34

Authors

Kandiah, E.,Gupta, K. (deposition date: 2016-10-19, release date: 2017-11-29, Last modification date: 2024-05-08)

Primary citation

Gupta, K.,Watson, A.A.,Baptista, T.,Scheer, E.,Chambers, A.L.,Koehler, C.,Zou, J.,Obong-Ebong, I.,Kandiah, E.,Temblador, A.,Round, A.,Forest, E.,Man, P.,Bieniossek, C.,Laue, E.D.,Lemke, E.A.,Rappsilber, J.,Robinson, C.V.,Devys, D.,Tora, L.,Berger, I.
Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID.
Elife, 6:-, 2017

PubMed Abstract: General transcription factor TFIID is a key component of RNA polymerase II transcription initiation. Human TFIID is a megadalton-sized complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. We identified a ternary complex formed by TBP and the histone fold (HF) domain-containing TFIID subunits TAF11 and TAF13. We demonstrate that TAF11/TAF13 competes for TBP binding with TATA-box DNA, and also with the N-terminal domain of TAF1 previously implicated in TATA-box mimicry. In an integrative approach combining crystal coordinates, biochemical analyses and data from cross-linking mass-spectrometry (CLMS), we determine the architecture of the TAF11/TAF13/TBP complex, revealing TAF11/TAF13 interaction with the DNA binding surface of TBP. We identify a highly conserved C-terminal TBP-interaction domain (CTID) in TAF13, which is essential for supporting cell growth. Our results thus have implications for cellular TFIID assembly and suggest a novel regulatory state for TFIID function.

PubMed: 29111974
DOI: 10.7554/eLife.30395

Experimental method

X-RAY DIFFRACTION (2.38 Å)