2G36

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

Han, G.W., Yang, X.L., McMullan, D., Chong, Y.E., Krishna, S.S., Rife, C.L., Weekes, D., Brittain, S.M., Abdubek, P., Ambing, E., Astakhova, T., Axelrod, H.L., Carlton, D., Caruthers, J., Chiu, H.J., Clayton, T., Duan, L., Feuerhelm, J., Grant, J.C., Grzechnik, S.K., Jaroszewski, L., Jin, K.K., Klock, H.E., Knuth, M.W., Kumar, A., Marciano, D., Miller, M.D., Morse, A.T., Nigoghossian, E., Okach, L., Paulsen, J., Reyes, R., van den Bedem, H., White, A., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J., Deacon, A.M., Godzik, A., Lesley, S.A., Elsliger, M.A., Schimmel, P., Wilson, I.A.

(2010) Acta Crystallogr Sect F Struct Biol Cryst Commun 66: 1326-1334

• PubMed: 20944229 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S1744309110037619
• Primary Citation of Related Structures:  
  2G36


• PubMed Abstract: 
  

  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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Organizational Affiliation: 

Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA, USA.