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PMID: 2011598 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 7 ·1991-04-01 ·Pages 2903-7

Perona JJ, Rould MA, Steitz TA, Risler JL, Zelwer C, Brunie S

Abstract

Detailed comparisons between the structures of the tRNA-bound Escherichia coli glutaminyl-tRNA (Gln-tRNA) synthetase [L-glutamine:tRNA(Gln) ligase (AMP-forming), EC 6.1.1.18] and recently refined E. coli methionyl-tRNA (Met-tRNA) synthetase [L-methionine:tRNA(Met) ligase (AMP-forming), EC 6.1.1.10] reveal significant similarities beyond the anticipated correspondence of their respective dinucleotide-fold domains. One similarity comprises a 23-amino acid alpha-helix-turn-beta-strand motif found in each enzyme within a domain that is inserted between the two halves of the dinucleotide binding fold. A second correspondence, which consists of two alpha-helices connected by a large loop and beta-strand, is located in the Gln-tRNA synthetase within a region that binds the inside corner of the "L"-shaped tRNA molecule. This structural motif contains a long alpha-helix, which extends along the entire length of the D and anticodon stems of the complexed tRNA. We suggest that the positioning of this helix relative to the dinucleotide fold plays a critical role in ensuring the proper global orientation of tRNA(Gln) on the surface of the enzyme. The structural correspondences suggest a similar overall orientation of binding of tRNA(Met) and tRNA(Gln) to their respective synthetases.

MeSH Terms
Amino Acyl-tRNA Synthetases/chemistry,metabolism Escherichia coli/enzymology Methionine-tRNA Ligase/chemistry,metabolism Models, Molecular Nucleic Acid Conformation Protein Conformation RNA, Transfer, Gln/chemistry,metabolism RNA, Transfer, Met/chemistry,metabolism
Chemicals
RNA, Transfer, Gln RNA, Transfer, Met Amino Acyl-tRNA Synthetases Methionine-tRNA Ligase glutaminyl-tRNA synthetase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Perona J J
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Rould M A
Steitz T A
Risler J L
Zelwer C
Brunie S
References (31)
31 references, click to expand
  1. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution.
    Science. 1989 Dec 1;246(4934):1135-42 PMID: 2479982
  2. Isolation and characterization of the gene coding for Escherichia coli arginyl-tRNA synthetase.
    Nucleic Acids Res. 1989 Jul 25;17(14):5725-36 PMID: 2668891
  3. Identification of the tRNA anticodon recognition site of Escherichia coli methionyl-tRNA synthetase.
    Biochemistry. 1990 Mar 6;29(9):2220-5 PMID: 2186810
  4. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs.
    Nature. 1990 Sep 13;347(6289):203-6 PMID: 2203971
  5. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
    Nature. 1990 Sep 20;347(6290):249-55 PMID: 2205803
  6. Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP.
    J Mol Biol. 1990 Nov 20;216(2):411-24 PMID: 2254937
  7. Selection of suppressor methionyl-tRNA synthetases: mapping the tRNA anticodon binding site.
    Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):291-5 PMID: 1986377
  8. Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate.
    J Mol Biol. 1989 Jul 5;208(1):83-98 PMID: 2504923
  9. Exploring structural homology of proteins.
    J Mol Biol. 1976 Jul 25;105(1):75-95 PMID: 186608
  10. The nucleotide sequence of the structural gene for Escherichia coli tryptophanyl-tRNA synthetase.
    J Biol Chem. 1982 Jun 10;257(11):6132-6 PMID: 7042706
  11. Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene.
    J Biol Chem. 1982 Oct 10;257(19):11639-43 PMID: 6288695
  12. Neutron scattering studies of escherichia coli tyrosyl-trna synthetase and of its interaction with trna tyr.
    J Mol Biol. 1982 Aug 25;159(4):651-64 PMID: 6754952
  13. The amino acid sequence of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus.
    Eur J Biochem. 1983 May 2;132(2):383-7 PMID: 6840095
  14. Primary structure of the Saccharomyces cerevisiae gene for methionyl-tRNA synthetase.
    Proc Natl Acad Sci U S A. 1983 May;80(9):2437-41 PMID: 6341994
  15. Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene.
    J Bacteriol. 1984 Dec;160(3):1115-22 PMID: 6094501
  16. Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase.
    Science. 1984 Dec 14;226(4680):1315-7 PMID: 6390679
  17. Methionyl-tRNA synthetase from Escherichia coli: primary structure at the binding site for the 3'-end of tRNAfMet.
    Biochemistry. 1985 Feb 26;24(5):1175-80 PMID: 3913464
  18. Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases.
    J Biol Chem. 1986 Aug 15;261(23):10610-7 PMID: 3015933
  19. Identification of peptide sequences at the tRNA binding site of Escherichia coli methionyl-tRNA synthetase.
    Biochemistry. 1986 Aug 12;25(16):4555-61 PMID: 3094575
  20. Sequence similarities among the family of aminoacyl-tRNA synthetases.
    Biochimie. 1986 Sep;68(9):1071-8 PMID: 3096385
  21. Topographic modeling of free and methionyl-tRNA synthetase bound tRNAfMet by singlet-singlet energy transfer: bending of the 3'-terminal arm in tRNAfMet.
    Biochemistry. 1986 Oct 21;25(21):6572-8 PMID: 3641634
  22. Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs.
    Annu Rev Biochem. 1987;56:125-58 PMID: 3304131
  23. tRNA recognition site of Escherichia coli methionyl-tRNA synthetase.
    Biochemistry. 1987 Aug 25;26(17):5416-22 PMID: 3118944
  24. Nucleotide sequence of Escherichia coli valyl-tRNA synthetase gene valS.
    Nucleic Acids Res. 1987 Nov 11;15(21):9081-2 PMID: 3317277
  25. Valyl-tRNA synthetase gene of Escherichia coli K12. Primary structure and homology within a family of aminoacyl-TRNA synthetases.
    J Biol Chem. 1988 Jan 15;263(2):868-77 PMID: 3275660
  26. Molecular cloning and nucleotide sequence of the gene for Escherichia coli leucyl-tRNA synthetase.
    Nucleic Acids Res. 1987 Dec 23;15(24):10199-210 PMID: 3320963
  27. Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activity.
    Biochemistry. 1988 Jul 26;27(15):5525-30 PMID: 3179266
  28. Anticodon switching changes the identity of methionine and valine transfer RNAs.
    Science. 1988 Nov 4;242(4879):765-8 PMID: 3055296
  29. Characterization of MSM1, the structural gene for yeast mitochondrial methionyl-tRNA synthetase.
    Eur J Biochem. 1989 Feb 1;179(2):365-71 PMID: 2645139
  30. Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
    J Mol Biol. 1989 Feb 20;205(4):729-35 PMID: 2467006
  31. Insertion of new sequences into the catalytic domain of an enzyme.
    Biochemistry. 1989 Oct 17;28(21):8479-84 PMID: 2690943
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.7.2903
Published
1991-04-01
Pages
2903-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC51348
Subset
IM
Grants
NIGMS NIH HHS · GM-22778 · United States
External Links
PubMed source DOI: 10.1073/pnas.88.7.2903 PMC Full Text View journal details
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