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

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 6
Structure-based sequence alignment of TrpRSs. The four Cys residues in the C-x₂₂-C-x₆-C-x₂-C motif of TmTrpRS that chelate the [4Fe–4S] cluster are colored by red letters. Strictly conserved residues are highlighted in red boxes and additional conserved residues are in yellow boxes. The secondary-structure elements of TmTrpRS are shown at the top, where α-helices (α1–α15), β-strands (β1–β5) and 3₁₀-helices (η1–η4) are sequentially labeled and β-turns and γ-turns are designated with the Greek letter tau (T). Asp136, which is conserved among prokaryotes, is indicated with a blue diamond. Abbreviations: Thermotoga maritima TrpRS, TmTrpRS; Deinoccoccus radiodurans TrpRS_I, Dr_I; Bacillus stearothermophilus TrpRS, Bs; D. radiodurans TrpRS_II, Dr_II; Homo sapiens TrpRS, Hs. Note: the sequence of DrTrpRS_I is included in the alignment although there is no crystal structure available from the PDB.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309110037619

Follow Acta Cryst. F

Search term		doi		Advanced search
Author		volume	page