Literature DB >> 2207145

Structural determination of the functional sites of E. coli elongation factor Tu.

B F Clark1, M Kjeldgaard, T F la Cour, S Thirup, J Nyborg.   

Abstract

Recently, we have made significant progress in solving the structure of a nicked form of elongation factor (EF)-Tu complexed with GDP. The structure has been refined to an R factor of 19.2% at 2.6 A resolution, so that most of the structure is clearly visible in the electron density map. Here we describe what is known about functional sites of EF-Tu in terms of the structure, which still lacks amino acids 40-60.

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Year:  1990        PMID： 2207145     DOI： 10.1016/0167-4781(90)90167-z

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  11 in total

Review 1.  Functional sites in F1-ATPases: location and interactions.

Authors:  W S Allison; J M Jault; S Zhuo; S R Paik
Journal:  J Bioenerg Biomembr       Date:  1992-10       Impact factor: 2.945

2.  Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts.

Authors:  M E Peter; C O Reiser; N K Schirmer; T Kiefhaber; G Ott; N W Grillenbeck; M Sprinzl
Journal:  Nucleic Acids Res       Date:  1990-12-11       Impact factor: 16.971

3.  GTPase domains of ras p21 oncogene protein and elongation factor Tu: analysis of three-dimensional structures, sequence families, and functional sites.

Authors:  A Valencia; M Kjeldgaard; E F Pai; C Sander
Journal:  Proc Natl Acad Sci U S A       Date:  1991-06-15       Impact factor: 11.205

4.  The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny.

Authors:  S L Baldauf; J D Palmer; W F Doolittle
Journal:  Proc Natl Acad Sci U S A       Date:  1996-07-23       Impact factor: 11.205

5.  The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome.

Authors:  E Vorstenbosch; T Pape; M V Rodnina; B Kraal; W Wintermeyer
Journal:  EMBO J       Date:  1996-12-02       Impact factor: 11.598

6.  A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome.

Authors:  I Tubulekas; D Hughes
Journal:  J Bacteriol       Date:  1993-01       Impact factor: 3.490

Review 7.  A model for the catalytic site of F1-ATPase based on analogies to nucleotide-binding domains of known structure.

Authors:  T M Duncan; R L Cross
Journal:  J Bioenerg Biomembr       Date:  1992-10       Impact factor: 2.945

8.  F-actin sequesters elongation factor 1alpha from interaction with aminoacyl-tRNA in a pH-dependent reaction.

Authors:  G Liu; J Tang; B T Edmonds; J Murray; S Levin; J Condeelis
Journal:  J Cell Biol       Date:  1996-11       Impact factor: 10.539

9.  Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome.

Authors:  M V Rodnina; R Fricke; L Kuhn; W Wintermeyer
Journal:  EMBO J       Date:  1995-06-01       Impact factor: 11.598

10.  Elongation factor Tu is a multifunctional and processed moonlighting protein.

Authors:  Michael Widjaja; Kate Louise Harvey; Lisa Hagemann; Iain James Berry; Veronica Maria Jarocki; Benjamin Bernard Armando Raymond; Jessica Leigh Tacchi; Anne Gründel; Joel Ricky Steele; Matthew Paul Padula; Ian George Charles; Roger Dumke; Steven Philip Djordjevic
Journal:  Sci Rep       Date:  2017-09-11       Impact factor: 4.379
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