Journal of Structural and Functional Genomics

, Volume 13, Issue 4, pp 233–239

The crystal structures of the α-subunit of the α2β2 tetrameric Glycyl-tRNA synthetase

Authors

  • Kemin Tan
    • Center for Structural Genomics of Infectious DiseasesUniversity of Chicago
    • Computation InstituteUniversity of Chicago
    • Structural Biology CenterBiosciences, Argonne National Laboratory
  • Min Zhou
    • Center for Structural Genomics of Infectious DiseasesUniversity of Chicago
    • Computation InstituteUniversity of Chicago
  • Rongguang Zhang
    • Center for Structural Genomics of Infectious DiseasesUniversity of Chicago
    • Computation InstituteUniversity of Chicago
    • Structural Biology CenterBiosciences, Argonne National Laboratory
  • Wayne F. Anderson
    • Center for Structural Genomics of Infectious DiseasesUniversity of Chicago
    • Molecular Pharmacology and Biological ChemistryNorthwestern University
    • Center for Structural Genomics of Infectious DiseasesUniversity of Chicago
    • Computation InstituteUniversity of Chicago
    • Structural Biology CenterBiosciences, Argonne National Laboratory
Article

DOI: 10.1007/s10969-012-9142-6

Cite this article as:
Tan, K., Zhou, M., Zhang, R. et al. J Struct Funct Genomics (2012) 13: 233. doi:10.1007/s10969-012-9142-6

Abstract

Aminoacyl-tRNA synthetases (AARSs) are ligases (EC.6.1.1.-) that catalyze the acylation of amino acids to their cognate tRNAs in the process of translating genetic information from mRNA to protein. Their amino acid and tRNA specificity are crucial for correctly translating the genetic code. Glycine is the smallest amino acid and the glycyl-tRNA synthetase (GlyRS) belongs to Class II AARSs. The enzyme is unusual because it can assume different quaternary structures. In eukaryotes, archaebacteria and some bacteria, it forms an α2 homodimer. In some bacteria, GlyRS is an α2β2 heterotetramer and shows a distant similarity to α2 GlyRSs. The human pathogen eubacterium Campylobacter jejuni GlyRS (CjGlyRS) is an α2β2 heterotetramer and is similar to Escherichia coli GlyRS; both are members of Class IIc AARSs. The two-step aminoacylation reaction of tetrameric GlyRSs requires the involvement of both α- and β-subunits. At present, the structure of the GlyRS α2β2 class and the details of the enzymatic mechanism of this enzyme remain unknown. Here we report the crystal structures of the catalytic α-subunit of CjGlyRS and its complexes with ATP, and ATP and glycine. These structures provide detailed information on substrate binding and show evidence for a proposed mechanism for amino acid activation and the formation of the glycyl-adenylate intermediate for Class II AARSs.

Keywords

Gly-tRNA synthetase Catalytic subunit ATP binding Glycine binding

Copyright information

© Springer Science+Business Media B.V. (outside the USA)  2012