4B0A

The high-resolution structure of yTBP-yTAF1 identifies conserved and competing interaction surfaces in transcriptional activation

Summary for 4B0A

• Entry DOI: 10.2210/pdb4b0a/pdb
• Related: 1NGM 1NH2 1RM1 1TBA 1TBP 1YTB 1YTF
• Descriptor: TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1, LINKER, TATA-BOX-BINDING PROTEIN, CALCIUM ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: transcription
• Biological source: SACCHAROMYCES CEREVISIAE
• Cellular location: Nucleus: P13393
• Total number of polymer chains: 1
• Total formula weight: 31024.61

Authors

Anandapadamanaban, M.,Andresen, C.,Siponen, M.,Kokubo, T.,Ikura, M.,Moche, M.,Sunnerhagen, M. (deposition date: 2012-06-29, release date: 2013-07-03, Last modification date: 2023-12-20)

Primary citation

Anandapadamanaban, M.,Andresen, C.,Siponen, M.,Kokubo, T.,Ikura, M.,Moche, M.,Sunnerhagen, M.
High-Resolution Structure of TBP with Taf1 Reveals Anchoring Patterns in Transcriptional Regulation
Nat.Struct.Mol.Biol., 20:1008-, 2013

PubMed Abstract: The general transcription factor TFIID provides a regulatory platform for transcription initiation. Here we present the crystal structure (1.97 Å) and NMR analysis of yeast TAF1 N-terminal domains TAND1 and TAND2 bound to yeast TBP, together with mutational data. We find that yeast TAF1-TAND1, which in itself acts as a transcriptional activator, binds TBP's concave DNA-binding surface by presenting similar anchor residues to TBP as does Mot1 but from a distinct structural scaffold. Furthermore, we show how TAF1-TAND2 uses an aromatic and acidic anchoring pattern to bind a conserved TBP surface groove traversing the basic helix region, and we find highly similar TBP-binding motifs also presented by the structurally distinct TFIIA, Mot1 and Brf1 proteins. Our identification of these anchoring patterns, which can be easily disrupted or enhanced, provides insight into the competitive multiprotein TBP interplay critical to transcriptional regulation.

PubMed: 23851461
DOI: 10.1038/NSMB.2611

Experimental method

X-RAY DIFFRACTION (1.97 Å)