PDBsum entry 2kis

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Transcription regulator PDB id
Protein chain
71 a.a. *
* Residue conservation analysis
PDB id:
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 DOI: 10.1016/j.jmb.2009.08.049
08-May-09     Release date:   08-Sep-09    
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Protein chain
Pfam   ArchSchema ?
O14776  (TCRG1_HUMAN) -  Transcription elongation regulator 1
1098 a.a.
71 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)


DOI no: 10.1016/j.jmb.2009.08.049 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.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20174897 S.Yao, J.M.Murphy, A.Low, and R.S.Norton (2010).
1H, 13C and 15N resonance assignments of a highly-soluble murine interleukin-3 analogue with wild-type bioactivity.
  Biomol NMR Assign, 4, 73-77.  
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