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PDBsum entry 1tfe
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Elongation factor PDB id
1tfe

 

 

 

 

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Contents
Protein chain
142 a.a. *
Waters ×777
* Residue conservation analysis
PDB id:
1tfe
Name: Elongation factor
Title: Dimerization domain of ef-ts from t. Thermophilus
Structure: Elongation factor ts. Chain: a. Fragment: ef-ts dimerization domain, residues 55 - 196. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 274. Cell_line: bl21. Gene: tsf. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
Resolution:
1.70Å     R-factor:   0.207     R-free:   0.285
Authors: Y.Jiang,S.Nock,M.Nesper,M.Sprinzl,P.B.Sigler
Key ref:
Y.Jiang et al. (1996). Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus. Biochemistry, 35, 10269-10278. PubMed id: 8756682 DOI: 10.1021/bi960918w
Date:
16-Apr-96     Release date:   08-Nov-96    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P43895  (EFTS_THET8) -  Elongation factor Ts from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Seq:
Struc: 		196 a.a.
142 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1021/bi960918w Biochemistry 35:10269-10278 (1996)
PubMed id: 8756682  
 
 
Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus.
Y.Jiang, S.Nock, M.Nesper, M.Sprinzl, P.B.Sigler.
 
  ABSTRACT  
 
Elongation factor Ts (EF-Ts) functions as a nucleotide-exchange factor by binding elongation factor Tu (EF-Tu) and accelerating the GDP dissociation from EF-Tu; thus EF-Ts promotes the transition of EF-Tu from the inactive GDP form to the active GTP form. Thermus thermophilus EF-Ts exists as a stable dimer in solution which binds two molecules of EF-Tu to form a (EF-Tu.EF-Ts)2 heterotetramer. Here we report the crystal structure of the dimerization domain of EF-Ts from T. thermophilus refined to 1.7 A resolution. A three-stranded antiparallel beta-sheet from each subunit interacts to form a beta-sandwich that serves as an extensive dimer interface tethered by a disulfide bond. This interface is distinctly different from the predominantly alpha-helical one that stabilizes the EF-Ts dimer from Escherichia coli [Kawashima, T., et al. (1996) Nature 379, 511-518]. To test whether the homodimeric form of T. thermophilus EF-Ts is necessary for catalyzing nucleotide exchange, the present structure was used to design mutational changes within the dimer interface that disrupt the T. thermophilus EF-Ts dimer but not the tertiary structure of the subunits. Surprisingly, EF-Ts monomers created in this manner failed to catalyze nucleotide exchange in EF-Tu, indicating that, in vitro. T. thermophilus EF-Ts functions only as a homodimer.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18513746 N.P.King, T.M.Lee, M.R.Sawaya, D.Cascio, and T.O.Yeates (2008).
Structures and functional implications of an AMP-binding cystathionine beta-synthase domain protein from a hyperthermophilic archaeon.
  J Mol Biol, 380, 181-192.
PDB codes: 2rif 2rih
15557323 M.G.Jeppesen, T.Navratil, L.L.Spremulli, and J.Nyborg (2005).
Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex.
  J Biol Chem, 280, 5071-5081.
PDB code: 1xb2
16151092 T.Kaper, B.Talik, T.J.Ettema, H.Bos, M.J.van der Maarel, and L.Dijkhuizen (2005).
Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels.
  Appl Environ Microbiol, 71, 5098-5106.  
12107280 P.Mallick, D.R.Boutz, D.Eisenberg, and T.O.Yeates (2002).
Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds.
  Proc Natl Acad Sci U S A, 99, 9679-9684.  
11500369 M.E.Kimple, D.P.Siderovski, and J.Sondek (2001).
Functional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpA.
  EMBO J, 20, 4414-4422.
PDB code: 1ihj
11489901 T.C.Appleby, I.I.Mathews, M.Porcelli, G.Cacciapuoti, and S.E.Ealick (2001).
Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus.
  J Biol Chem, 276, 39232-39242.
PDB codes: 1jds 1jdt 1jdu 1jdv 1jdz 1je0 1je1 1jp7 1jpv
10368293 M.Singleton, M.Isupov, and J.Littlechild (1999).
X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis.
  Structure, 7, 237-244.
PDB code: 1a2z
9032056 B.F.Clark, and J.Nyborg (1997).
The ternary complex of EF-Tu and its role in protein biosynthesis.
  Curr Opin Struct Biol, 7, 110-116.  
9253415 Y.Wang, Y.Jiang, M.Meyering-Voss, M.Sprinzl, and P.B.Sigler (1997).
Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.
  Nat Struct Biol, 4, 650-656.
PDB code: 1aip
9256058 Y.Watanabe, K.Kita, T.Ueda, and K.Watanabe (1997).
cDNA sequence of a translational elongation factor Ts homologue from Caenorhabditis elegans: mitochondrial factor-specific features found in the nematode homologue peptide.
  Biochim Biophys Acta, 1353, 7.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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