2NXP

Structure of NTD2 domain of the human TAF5 subunit of TFIID

Summary for 2NXP

• Entry DOI: 10.2210/pdb2nxp/pdb
• Descriptor: Transcription initiation factor TFIID subunit 5, CALCIUM ION (3 entities in total)
• Functional Keywords: transcription factor, tfiid subunit, taf5, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q15542
• Total number of polymer chains: 8
• Total formula weight: 151060.11

Authors

Bhattacharya, S.,Takada, S.,Jacobson, R.H. (deposition date: 2006-11-17, release date: 2007-01-09, Last modification date: 2024-11-20)

Primary citation

Bhattacharya, S.,Takada, S.,Jacobson, R.H.
Structural analysis and dimerization potential of the human TAF5 subunit of TFIID.
Proc.Natl.Acad.Sci.Usa, 104:1189-1194, 2007

PubMed Abstract: TFIID is an essential factor required for RNA polymerase II transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a structural analysis of the TAF5 protein. Our structure at 2.2-A resolution of the TAF5-NTD2 domain reveals an alpha-helical domain with distant structural similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain contains several conserved clefts likely to be critical for TFIID complex assembly. Our biochemical analysis of the human TAF5 protein demonstrates the ability of the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a key property required for the assembly of the TFIID complex.

PubMed: 17227857
DOI: 10.1073/pnas.0610297104

Experimental method

X-RAY DIFFRACTION (2.17 Å)