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