PDBsum entry 2pp4

Transcription

PDB id: 2pp4

Contents

Protein chain

107 a.a. *

* Residue conservation analysis

PDB id:

2pp4

Name:

Transcription

Title:

Solution structure of eto-tafh refined in explicit solvent

Structure:

Protein eto. Chain: a. Fragment: tafh domain, residues 119-225. Synonym: protein cbfa2t1, protein mtg8, eight twenty one protein, cyclin-d-related protein, zinc finger mynd domain- containing protein 2. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: runx1t1, aml1t1, cbfa2t1, cdr, eto, mtg8, zmynd2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

Y.Wei,S.Liu,J.Lausen,C.Woodrell,S.Cho,N.Biris,N.Kobayashi,S.Yokoyama, M.H.Werner

Key ref:

Y.Wei et al. (2007). A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription. Nat Struct Biol, 14, 653-661. PubMed id: 17572682 DOI: 10.1038/nsmb1258

Date:

27-Apr-07 Release date: 19-Jun-07

Protein chain

Q06455  (MTG8_HUMAN) -  Protein CBFA2T1 from Homo sapiens

Seq: 604 a.a.

Struc: 107 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nsmb1258

Nat Struct Biol 14:653-661 (2007)

PubMed id: 17572682

A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription.

Y.Wei, S.Liu, J.Lausen, C.Woodrell, S.Cho, N.Biris, N.Kobayashi, Y.Wei, S.Yokoyama, M.H.Werner.

ABSTRACT

The eight twenty-one protein, ETO, is implicated in 12%-15% of acute human leukemias as part of a gene fusion with RUNX1 (also called AML1). Of the four ETO domains related to Drosophila melanogaster Nervy, only two are required to induce spontaneous myeloid leukemia upon transplantation into the mouse. One of these domains is related in sequence to TAF4, a component of TFIID. The structure of this domain, ETO-TAFH, is similar to yeast Rpb4 and to Escherichia coli sigma(70); it is the first TAF-related protein with structural similarity to the multisubunit RNA polymerases. Overlapping surfaces of ETO-TAFH interact with an autonomous repression domain of the nuclear receptor corepressor N-CoR and with a conserved activation domain from the E-box family of transcription factors. Thus, ETO-TAFH acts as a structural platform that can interchange negative and positive coregulatory proteins to control transcription.

Selected figure(s)

Figure 2.
(a) Stereo superposition of the family of 20 ETO-TAFH structures. The structure is composed of five helices, H1–H5. The longest helix, H4, is kinked by 30° owing to the presence of Pro190 in the middle of the helix. (b) Cylindrical representation of ETO-TAFH in the same orientation as in a, indicating the positions of the five helices.

Figure 6.
(a) Cluster analysis of the N-CoR-R1 complex with ETO-TAFH. Two clusters are seen, with the lowest-energy cluster circled, representing 75% of the 200 water-refined structures from HADDOCK (see Methods). (b) Stereo view of representative model from the lowest-energy cluster in a. Black band, Leu387 of N-CoR-R1. Light shading, positions of mutations in ETO-TAFH that disrupt interaction with N-CoR-R1 or HEB-AD1, as discussed in the text.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2007, 14, 653-661) copyright 2007.

Figures were selected by an automated process.