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. Author manuscript; available in PMC: 2011 Jul 9.
Published in final edited form as: J Mol Biol. 2010 May 7;400(2):204–217. doi: 10.1016/j.jmb.2010.05.003

Figure 7.

Figure 7

Active-site structural similarities between AdoMet-dependent methyl transferases and ATP-dependent aminoacyl-tRNA synthetases. (A) Active site of M. jannaschii Trm5 in complex with AdoMet (PDB ID:2ZZN) 9. (B) Active site of Haemophilus influenzae TrmD in complex with AdoMet (PDB ID:1UAK) 4. (C) Active site of the class I E. coli GlnRS in complex with ATP complex (PDB ID:1GTR) 26. (D) Active site of the class II Pyrococcus kodakaraensis AspRS in complex with a U-shaped ATP (PDB ID:1B8A) 51. All structures show the conserved residues that stabilize the specific conformation of the cofactor, which exhibits an extended conformation in (A) and (C) and in a U-shaped conformation in (B) and (D).