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PDBsum entry 3hfh

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protein Protein-protein interface(s) links
Transcription regulator PDB id
3hfh
Jmol
Contents
Protein chains
168 a.a.
190 a.a.
Waters ×55
PDB id:
3hfh
Name: Transcription regulator
Title: Crystal structure of tandem ff domains
Structure: Transcription elongation regulator 1. Chain: a, b. Fragment: ff domains: unp residues 661-845. Synonym: tata box-binding protein-associated factor 2s, transcription factor ca150. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca150, taf2s, tcerg1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.70Å     R-factor:   0.235     R-free:   0.283
Authors: M.Lu,J.Yang,Z.Ren,S.Subir,M.T.Bedford,R.H.Jacobson, J.S.Mcmurray,X.Chen
Key ref:
M.Lu et al. (2009). Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150. J Mol Biol, 393, 397-408. PubMed id: 19660470 DOI: 10.1016/j.jmb.2009.07.086
Date:
11-May-09     Release date:   18-Aug-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O14776  (TCRG1_HUMAN) -  Transcription elongation regulator 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1098 a.a.
168 a.a.*
Protein chain
Pfam   ArchSchema ?
O14776  (TCRG1_HUMAN) -  Transcription elongation regulator 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1098 a.a.
190 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 62 residue positions (black crosses)

 

 
DOI no: 10.1016/j.jmb.2009.07.086 J Mol Biol 393:397-408 (2009)
PubMed id: 19660470  
 
 
Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150.
M.Lu, J.Yang, Z.Ren, S.Sabui, A.Espejo, M.T.Bedford, R.H.Jacobson, D.Jeruzalmi, J.S.McMurray, X.Chen.
 
  ABSTRACT  
 
FF domains are small protein-protein interaction modules that have two flanking conserved phenylalanine residues. They are present in proteins involved in transcription, RNA splicing, and signal transduction, and often exist in tandem arrays. Although several individual FF domain structures have been determined by NMR, the tandem nature of most FF domains has not been revealed. Here we report the 2.7-A-resolution crystal structure of the first three FF domains of the human transcription elongation factor CA150. Each FF domain is composed of three alpha-helices and a 3(10) helix between alpha-helix 2 and alpha-helix 3. The most striking feature of the structure is that an FF domain is connected to the next by an alpha-helix that continues from helix 3 to helix 1 of the next. The consequent elongated arrangement allows exposure of many charged residues within the region that can be engaged in interaction with other molecules. Binding studies using a peptide ligand suggest that a specific conformation of the FF domains might be required to achieve higher-affinity binding. Additionally, we explore potential DNA binding of the FF construct used in this study. Overall, we provide the first crystal structure of an FF domain and insights into the tandem nature of the FF domains and suggest that, in addition to protein binding, FF domains might be involved in DNA binding.
 
  Selected figure(s)  
 
Figure 3.
Fig. 3. Overall structure of CA150 FF1–3. (a–c) “Cartoon” diagrams of the structure related by ± 90° rotations along the x-axis. FF domains (boundaries defined in Fig. 1b) are shown in red, and connectors are shown in green. The dimensions of the structure and the cross angle of the two connector helices are indicated. (d) Superimposition of the NMR structures of CA150 FF1 (cyan), FF2 (magenta), and FF3 (yellow) onto the crystal structure of FF1–3 (green; same orientation as in Fig. 3b). The termini of the NMR structures are labeled by their corresponding residues.
Figure 4.
Fig. 4. Electrostatic properties of FF1–3. (a) “Cartoon” diagram showing the location of the charged residues on the protein. Positively (KR) and negatively (DE) charged residues are shown in blue and red, respectively, whereas the other residues are shown in lighter colors.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2009, 393, 397-408) copyright 2009.  
  Figures were selected by an automated process.