Skip to main content
PMC home page
Protein Science : A Publication of the Protein Society logoLink to Protein Science : A Publication of the Protein Society
. 1993 Dec;2(12):2259–2262. doi: 10.1002/pro.5560021225

Idiographic representation of conserved domain of a class II tRNA synthetase of unknown structure.

L Ribas de Pouplana 1, D D Buechter 1, M W Davis 1, P Schimmel 1
PMCID: PMC2142315  PMID: 8298469

Full Text

The Full Text of this article is available as a PDF (462.0 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Brick P., Bhat T. N., Blow D. M. 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. doi: 10.1016/0022-2836(89)90090-9. [DOI] [PubMed] [Google Scholar]
  2. Brunie S., Zelwer C., Risler J. L. 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):411–424. doi: 10.1016/S0022-2836(05)80331-6. [DOI] [PubMed] [Google Scholar]
  3. Buechter D. D., Schimmel P. Dissection of a class II tRNA synthetase: determinants for minihelix recognition are tightly associated with domain for amino acid activation. Biochemistry. 1993 May 18;32(19):5267–5272. doi: 10.1021/bi00070a039. [DOI] [PubMed] [Google Scholar]
  4. Cavarelli J., Rees B., Ruff M., Thierry J. C., Moras D. Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature. 1993 Mar 11;362(6416):181–184. doi: 10.1038/362181a0. [DOI] [PubMed] [Google Scholar]
  5. Chang P. K., Dignam J. D. Primary structure of alanyl-tRNA synthetase and the regulation of its mRNA levels in Bombyx mori. J Biol Chem. 1990 Dec 5;265(34):20898–20906. [PubMed] [Google Scholar]
  6. Cusack S., Berthet-Colominas C., Härtlein M., Nassar N., Leberman R. 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):249–255. doi: 10.1038/347249a0. [DOI] [PubMed] [Google Scholar]
  7. Cusack S., Härtlein M., Leberman R. Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res. 1991 Jul 11;19(13):3489–3498. doi: 10.1093/nar/19.13.3489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Eriani G., Delarue M., Poch O., Gangloff J., Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 1990 Sep 13;347(6289):203–206. doi: 10.1038/347203a0. [DOI] [PubMed] [Google Scholar]
  9. Francklyn C., Schimmel P. Aminoacylation of RNA minihelices with alanine. Nature. 1989 Feb 2;337(6206):478–481. doi: 10.1038/337478a0. [DOI] [PubMed] [Google Scholar]
  10. Francklyn C., Shi J. P., Schimmel P. Overlapping nucleotide determinants for specific aminoacylation of RNA microhelices. Science. 1992 Feb 28;255(5048):1121–1125. doi: 10.1126/science.1546312. [DOI] [PubMed] [Google Scholar]
  11. Hill K., Schimmel P. Evidence that the 3' end of a tRNA binds to a site in the adenylate synthesis domain of an aminoacyl-tRNA synthetase. Biochemistry. 1989 Mar 21;28(6):2577–2586. doi: 10.1021/bi00432a035. [DOI] [PubMed] [Google Scholar]
  12. Jasin M., Regan L., Schimmel P. Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase. Nature. 1983 Dec 1;306(5942):441–447. doi: 10.1038/306441a0. [DOI] [PubMed] [Google Scholar]
  13. Musier-Forsyth K., Scaringe S., Usman N., Schimmel P. Enzymatic aminoacylation of single-stranded RNA with an RNA cofactor. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):209–213. doi: 10.1073/pnas.88.1.209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Park S. J., Hou Y. M., Schimmel P. A single base pair affects binding and catalytic parameters in the molecular recognition of a transfer RNA. Biochemistry. 1989 Mar 21;28(6):2740–2746. doi: 10.1021/bi00432a056. [DOI] [PubMed] [Google Scholar]
  15. Putney S. D., Royal N. J., Neuman de Vegvar H., Herlihy W. C., Biemann K., Schimmel P. Primary structure of a large aminoacyl-tRNA synthetase. Science. 1981 Sep 25;213(4515):1497–1501. doi: 10.1126/science.7025207. [DOI] [PubMed] [Google Scholar]
  16. Putney S. D., Sauer R. T., Schimmel P. R. Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits. J Biol Chem. 1981 Jan 10;256(1):198–204. [PubMed] [Google Scholar]
  17. Regan L., Bowie J., Schimmel P. Polypeptide sequences essential for RNA recognition by an enzyme. Science. 1987 Mar 27;235(4796):1651–1653. doi: 10.1126/science.2435005. [DOI] [PubMed] [Google Scholar]
  18. Rost B., Sander C. Jury returns on structure prediction. Nature. 1992 Dec 10;360(6404):540–540. doi: 10.1038/360540b0. [DOI] [PubMed] [Google Scholar]
  19. Rould M. A., Perona J. J., Söll D., Steitz T. A. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution. Science. 1989 Dec 1;246(4934):1135–1142. doi: 10.1126/science.2479982. [DOI] [PubMed] [Google Scholar]
  20. Ruff M., Krishnaswamy S., Boeglin M., Poterszman A., Mitschler A., Podjarny A., Rees B., Thierry J. C., Moras D. Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science. 1991 Jun 21;252(5013):1682–1689. doi: 10.1126/science.2047877. [DOI] [PubMed] [Google Scholar]
  21. Schimmel P. RNA minihelices and the decoding of genetic information. FASEB J. 1991 May;5(8):2180–2187. doi: 10.1096/fasebj.5.8.2022314. [DOI] [PubMed] [Google Scholar]
  22. Seeman N. C., Rosenberg J. M., Rich A. Sequence-specific recognition of double helical nucleic acids by proteins. Proc Natl Acad Sci U S A. 1976 Mar;73(3):804–808. doi: 10.1073/pnas.73.3.804. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Selbitschka W., Arnold W., Priefer U. B., Rottschäfer T., Schmidt M., Simon R., Pühler A. Characterization of recA genes and recA mutants of Rhizobium meliloti and Rhizobium leguminosarum biovar viciae. Mol Gen Genet. 1991 Sep;229(1):86–95. doi: 10.1007/BF00264217. [DOI] [PubMed] [Google Scholar]
  24. Shi J. P., Martinis S. A., Schimmel P. RNA tetraloops as minimalist substrates for aminoacylation. Biochemistry. 1992 Jun 2;31(21):4931–4936. doi: 10.1021/bi00136a002. [DOI] [PubMed] [Google Scholar]
  25. Steitz T. A. Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding. Q Rev Biophys. 1990 Aug;23(3):205–280. doi: 10.1017/s0033583500005552. [DOI] [PubMed] [Google Scholar]

Articles from Protein Science : A Publication of the Protein Society are provided here courtesy of The Protein Society

RESOURCES