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.

doi:10.1107/S1744309110037619

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 5
Enzymatic activities of TmTrpRS. (a) Aminoacylation activity assayed at 310 and 333 K. Consistent with its thermophilic nature, TmTrpRS has a more robust tRNA-charging activity at 333 K compared with that at 310 K. Control reaction assays lacking enzyme or tRNA at 333 K are also shown. Points are the mean of two assays and error bars represent the standard error of the mean of measurements. (b) ATP–PP_i-exchange activities assayed at 310 and 333 K. This experiment was only performed once. Plots were derived by fitting to an exponential rise to maximum function. Control reaction assays lacking enzyme or Trp at 333 K are also shown. Consistent with the observation of an endogenously bound Trp molecule in the active site of its crystal structure, TmTrpRS had some PP_i-exchange activity even when no Trp was added to the reaction.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| September 2010| Pages 1326-1334

doi:10.1107/S1744309110037619

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