PDBsum entry 3aad

Transcription/chaperone

PDB id: 3aad

Contents

Protein chains

264 a.a. *

153 a.a. *

Ligands

SO4

* Residue conservation analysis

PDB id:

3aad

Name:

Transcription/chaperone

Title:

Structure of the histone chaperone cia/asf1-double bromodomain complex linking histone modifications and site-specific histone eviction

Structure:

Transcription initiation factor tfiid subunit 1. Chain: a. Fragment: bromodomain. Synonym: transcription initiation factor tfiid 250 kda subunit, taf(ii)250, tafii-250, tafii250, tbp-associated factor 250 kda, p250, cell cycle gene 1 protein. Engineered: yes. Histone chaperone asf1a. Chain: b, d.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ccg1, taf1, tafii250. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: asf1a, cia-i.

Resolution:

3.30Å R-factor: 0.240 R-free: 0.293

Authors:

Y.Akai,N.Adachi,Y.Hayashi,M.Eitoku,N.Sano,R.Natsume,N.Kudo, M.Tanokura,T.Senda,M.Horikoshi

Key ref:

Y.Akai et al. (2010). Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction. Proc Natl Acad Sci U S A, 107, 8153-8158. PubMed id: 20393127

Date:

16-Nov-09 Release date: 28-Apr-10

Protein chain

P21675  (TAF1_HUMAN) -  Transcription initiation factor TFIID subunit 1 from Homo sapiens

Seq: 1893 a.a.

Struc: 264 a.a.

Protein chains

Q9Y294  (ASF1A_HUMAN) -  Histone chaperone ASF1A from Homo sapiens

Seq: 204 a.a.

Struc: 153 a.a.

Enzyme reactions

• Enzyme class 2: Chain A: E.C.2.3.1.48 - histone acetyltransferase.
• Reaction: L-lysyl-[protein] + acetyl-CoA = N₆-acetyl-L-lysyl-[protein] + CoA + H⁺
• Enzyme class 3: Chain A: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Proc Natl Acad Sci U S A 107:8153-8158 (2010)

PubMed id: 20393127

Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction.

Y.Akai, N.Adachi, Y.Hayashi, M.Eitoku, N.Sano, R.Natsume, N.Kudo, M.Tanokura, T.Senda, M.Horikoshi.

ABSTRACT

Nucleosomes around the promoter region are disassembled for transcription in response to various signals, such as acetylation and methylation of histones. Although the interactions between histone-acetylation-recognizing bromodomains and factors involved in nucleosome disassembly have been reported, no structural basis connecting histone modifications and nucleosome disassembly has been obtained. Here, we determined at 3.3 A resolution the crystal structure of histone chaperone cell cycle gene 1 (CCG1) interacting factor A/antisilencing function 1 (CIA/ASF1) in complex with the double bromodomain in the CCG1/TAF1/TAF(II)250 subunit of transcription factor IID. Structural, biochemical, and biological studies suggested that interaction between double bromodomain and CIA/ASF1 is required for their colocalization, histone eviction, and pol II entry at active promoter regions. Furthermore, the present crystal structure has characteristics that can connect histone acetylation and CIA/ASF1-mediated histone eviction. These findings suggest that the molecular complex between CIA/ASF1 and the double bromodomain plays a key role in site-specific histone eviction at active promoter regions. The model we propose here is the initial structure-based model of the biological signaling from histone modifications to structural change of the nucleosome (hi-MOST model).