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The EMBO Journal (1998) 17, 2947–2960, doi:10.1093/emboj/17.10.2947

Table 1
The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid
Carmen Berthet-Colominas, Laurence Seignovert, Michael Härtlein, Morten Grotli, Stephen Cusack and Reuben Leberman
Table 1: Equivalent active site residues in asparaginyl- and aspartyl-tRNA synthetases
    AsnRSTT AspRSTT AspRSSCa Principal interaction
ATP 1 Arg208 Arg223 Arg325 alpha-phosphate
  2 Glu210 Glu225 Glu327 base N6
  3 His217 Arg231 His333 gamma-phosphate
  4 Leu218 Gln232 Met334 main chain to base
  5 Phe221 Phe235 Phe337 stacks with base
  6 Arg412 Arg431 Arg531 gamma-phosphate/base
Magnesium 7 Asp352 Asp469 Asp471 Mg-1 (H2O mediated)
  8 Glu361 Glu476 Glu478 Mg-1, Mg-2
Samarium 9 Glu313 – Glu427 with (7) and (8)
Amino acid 10 Glu164 Glu177 Glu281a alpha-amino group
  11 Ser185 Ser199 Ser301a alpha-amino group
  12 Gln187 Gln201 Gln303 alpha-amino group (not AspRS)
  13 Ala190 Lys204 Lys306 amino acid side chain (not AsnRS)
  14 Glu191 Gln205 Gln307 H-bonds with (12) and (18)
  15 Glu225 Asp239 Asp342 NH2 of asparagine Lys (13) in AspRS
  16 Glu227 Glu241 Glu344 stabilizes (17)
  17 Arg368 Arg483 Arg485 amino acid side chain
  18 His403 His522 His522 donor to (14)

aIn AspRSSC, only structures in the presence of tRNA are available, in which case certain residues such as Glu281 and Ser301 are found interacting with Ade76 of the tRNA rather than with the amino acid substrate (Cavarelli et al., 1994).
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