PDBsum entry 2nxp

Transcription

PDB id: 2nxp

Contents

Protein chains

(+ 2 more) 149 a.a. *

Metals

_CA ×8

Waters ×521

* Residue conservation analysis

PDB id:

2nxp

Name:

Transcription

Title:

Structure of ntd2 domain of the human taf5 subunit of tfiid

Structure:

Transcription initiation factor tfiid subunit 5. Chain: a, b, c, d, e, f, g, h. Fragment: n-terminal conserved domain 2 (ntd2). Synonym: transcription initiation factor tfiid 100 kda subunit, tafii, 100, tafii-100, tafii100. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: taf5. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.17Å R-factor: 0.215 R-free: 0.263

Authors:

S.Bhattacharya,S.Takada,R.H.Jacobson

Key ref:

S.Bhattacharya et al. (2007). Structural analysis and dimerization potential of the human TAF5 subunit of TFIID. Proc Natl Acad Sci U S A, 104, 1189-1194. PubMed id: 17227857 DOI: 10.1073/pnas.0610297104

Date:

17-Nov-06 Release date: 09-Jan-07

Protein chains

Q15542  (TAF5_HUMAN) -  Transcription initiation factor TFIID subunit 5 from Homo sapiens

Seq: 800 a.a.

Struc: 149 a.a.

DOI no: 10.1073/pnas.0610297104

Proc Natl Acad Sci U S A 104:1189-1194 (2007)

PubMed id: 17227857

Structural analysis and dimerization potential of the human TAF5 subunit of TFIID.

S.Bhattacharya, S.Takada, R.H.Jacobson.

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.

Selected figure(s)

Figure 1.
Fig. 1. Primary sequence organization of hTAF5. Schematic diagram of the domain structure present in human TAF5 where NTD1/LisH corresponds to LIS1 homology domain (29), NTD2 corresponds to the -helical domain reported here, and WD40 repeats are predicted to form a closed -propeller structure.

Figure 2.
Fig. 2. Structure of the hTAF5-NTD2 domain. (a) Diagram of the hTAF5-NTD2. (b) Top view of the -helical domain of the hTAF5-NTD2 showing the arrangement of the other helices around the central helix ( 3) in the crystal structure. All of the helices and the strands are labeled. Two views in a and b are related by rotation of 90° around a horizontal axis. (c) Topology diagram of the secondary structural elements of the hTAF5-NTD2 domain to show the arrangement of the helical bundle (front view) and the helical sheet (back view) of the crystal structure.

Figures were selected by an automated process.