Structure of a tryptophanyl-tRNA synthetase containing an iron–sulfur cluster

نویسندگان

  • Gye Won Han
  • Xiang-Lei Yang
  • Daniel McMullan
  • Yeeting E. Chong
  • S. Sri Krishna
  • Christopher L. Rife
  • Dana Weekes
  • Scott M. Brittain
  • Polat Abdubek
  • Eileen Ambing
  • Tamara Astakhova
  • Herbert L. Axelrod
  • Dennis Carlton
  • Jonathan Caruthers
  • Hsiu-Ju Chiu
  • Thomas Clayton
  • Lian Duan
  • Julie Feuerhelm
  • Joanna C. Grant
  • Slawomir K. Grzechnik
  • Lukasz Jaroszewski
  • Kevin K. Jin
  • Heath E. Klock
  • Mark W. Knuth
  • Abhinav Kumar
  • David Marciano
  • Mitchell D. Miller
  • Andrew T. Morse
  • Edward Nigoghossian
  • Linda Okach
  • Jessica Paulsen
  • Ron Reyes
  • Henry van den Bedem
  • Aprilfawn White
  • Guenter Wolf
  • Qingping Xu
  • Keith O. Hodgson
  • John Wooley
  • Ashley M. Deacon
  • Adam Godzik
  • Scott A. Lesley
  • Marc-André Elsliger
  • Paul Schimmel
  • Ian A. Wilson
چکیده

A novel aminoacyl-tRNA synthetase that contains an iron-sulfur cluster in the tRNA anticodon-binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl-tRNA synthetase; TrpRS; EC 6.1.1.2) reveals an iron-sulfur [4Fe-4S] cluster bound to the tRNA anticodon-binding (TAB) domain and an L-tryptophan ligand in the active site. None of the other T. maritima aminoacyl-tRNA synthetases (AARSs) contain this [4Fe-4S] cluster-binding motif (C-x₂₂-C-x₆-C-x₂-C). It is speculated that the iron-sulfur cluster contributes to the stability of TmTrpRS and could play a role in the recognition of the anticodon.

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عنوان ژورنال:

دوره 66  شماره 

صفحات  -

تاریخ انتشار 2010