PDBsum entry 2kis

Transcription regulator

PDB id: 2kis

Contents

Protein chain

71 a.a. *

* Residue conservation analysis

PDB id:

2kis

Name:

Transcription regulator

Title:

Solution structure of ca150 ff1 domain and ff1-ff2 interdomain linker

Structure:

Transcription elongation regulator 1. Chain: a. Fragment: ff1 domain: unp residues 659-724. Synonym: tata box-binding protein-associated factor 2s, transcription factor ca150, ca150, tcerg-1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ca150, taf2s, tcerg-1, tcerg1. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: n-terminal 6xhis tag cleaved using tev protease

NMR struc:

7 models

Authors:

J.M.Murphy,D.Hansen,S.Wiesner,D.Muhandiram,M.Borg,M.J.Smith, F.Sicheri,L.E.Kay,J.D.Forman-Kay,T.Pawson

Key ref:

J.M.Murphy et al. (2009). Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays. J Mol Biol, 393, 409-424. PubMed id: 19715701

Date:

08-May-09 Release date: 08-Sep-09

Protein chain

O14776  (TCRG1_HUMAN) -  Transcription elongation regulator 1 from Homo sapiens

Seq: 1098 a.a.

Struc: 71 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

J Mol Biol 393:409-424 (2009)

PubMed id: 19715701

Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays.

J.M.Murphy, D.F.Hansen, S.Wiesner, D.R.Muhandiram, M.Borg, M.J.Smith, F.Sicheri, L.E.Kay, J.D.Forman-Kay, T.Pawson.

ABSTRACT

FF domains are poorly understood protein interaction modules that are present within eukaryotic transcription factors, such as CA150 (TCERG-1). The CA150 FF domains have been shown to mediate interactions with the phosphorylated C-terminal domain of RNA polymerase II (phosphoCTD) and a multitude of transcription factors and RNA processing proteins, and may therefore have a central role in organizing transcription. FF domains occur in tandem arrays of up to six domains, although it is not known whether they adopt higher-order structures. We have used the CA150 FF1+FF2 domains as a model system to examine whether tandem FF domains form higher-order structures in solution using NMR spectroscopy. In the solution structure of FF1 fused to the linker that joins FF1 to FF2, we observed that the highly conserved linker peptide is ordered and forms a helical extension of helix alpha3, suggesting that the interdomain linker might have a role in orientating FF1 relative to FF2. However, examination of the FF1+FF2 domains using relaxation NMR experiments revealed that although these domains are not rigidly orientated relative to one another, they do not tumble independently. Thus, the FF1+FF2 structure conforms to a dumbbell-shape in solution, where the helical interdomain linker maintains distance between the two dynamic FF domains without cementing their relative orientations. This model for FF domain organization within tandem arrays suggests a general mechanism by which individual FF domains can manoeuvre to achieve optimal recognition of flexible binding partners, such as the intrinsically-disordered phosphoCTD.