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
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Figure 2
Comparison of TmTrpRS and DrTrpRS_II. (a) Structural superposition of TmTrpRS (gray), DrTrpRS_II + ATP and Mg (PDB code 1yid ; green) and DrTrpRS_II + Trp (PDB code 1yi8 ; blue). The bound ATP is shown as a stick model. The [4Fe–4S] cluster (orange and yellow), Mg ion (green sphere) and Trp (gray, red and blue) are shown as spheres. The DrTrpRS_II structures superimpose with TmTrpRS over 319 C^α atoms with an r.m.s.d. of ∼1.7 Å (45% sequence identity). (b) Electrostatic surface potential of TmTrpRS calculated with the program APBS (Baker et al., 2001

): positive potential is shown in blue (+3kTe⁻¹) and negative in red (−3kTe⁻¹). L-Tryptophan and the iron–sulfur cluster are shown as spheres. Note: the ATP-binding site is solvent-exposed, but the tryptophan and the iron–sulfur cluster are partially buried.

STRUCTURAL BIOLOGY
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ISSN: 2053-230X

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

doi:10.1107/S1744309110037619

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