The class II aminoacyl-tRNA synthetases and their active site: evolutionary conservation of an ATP binding site - PubMed (original) (raw)
Comparative Study
. 1995 May;40(5):499-508.
doi: 10.1007/BF00166618.
Affiliations
- PMID: 7783225
- DOI: 10.1007/BF00166618
Comparative Study
The class II aminoacyl-tRNA synthetases and their active site: evolutionary conservation of an ATP binding site
G Eriani et al. J Mol Evol. 1995 May.
Abstract
Previous sequence analyses have suggested the existence of two distinct classes of aminoacyl-tRNA synthetase. The partition was established on the basis of exclusive sets of sequence motifs (Eriani et al. [1990] Nature 347:203-306). X-ray studies have now well defined the structural basis of the two classes: the class I enzymes share with dehydrogenases and kinases the classic nucleotide binding fold called the Rossmann fold, whereas the class II enzymes possess a different fold, not found elsewhere, built around a six-stranded antiparallel beta-sheet. The two classes of synthetases catalyze the same global reaction that is the attachment of an amino acid to the tRNA, but differ as to where on the terminal adenosine of the tRNA the amino acid is placed: class I enzymes act on the 2' hydroxyl whereas the class II enzymes prefer the 3' hydroxyl group. The three-dimensional structure of aspartyl-tRNA synthetase from yeast, a typical class II enzyme, is described here, in relation to its function. The crucial role of the sequence motifs in substrate binding and enzyme structure is high-lighted. Overall these results underline the existence of an intimate evolutionary link between the aminoacyl-tRNA synthetases, despite their actual structural diversity.
Similar articles
- Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase.
Cavarelli J, Rees B, Ruff M, Thierry JC, Moras D. Cavarelli J, et al. Nature. 1993 Mar 11;362(6416):181-4. doi: 10.1038/362181a0. Nature. 1993. PMID: 8450889 - Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.
Cusack S, Härtlein M, Leberman R. Cusack S, et al. Nucleic Acids Res. 1991 Jul 11;19(13):3489-98. doi: 10.1093/nar/19.13.3489. Nucleic Acids Res. 1991. PMID: 1852601 Free PMC article. - Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp).
Ruff M, Krishnaswamy S, Boeglin M, Poterszman A, Mitschler A, Podjarny A, Rees B, Thierry JC, Moras D. Ruff M, et al. Science. 1991 Jun 21;252(5013):1682-9. doi: 10.1126/science.2047877. Science. 1991. PMID: 2047877 - Structural and functional relationships between aminoacyl-tRNA synthetases.
Moras D. Moras D. Trends Biochem Sci. 1992 Apr;17(4):159-64. doi: 10.1016/0968-0004(92)90326-5. Trends Biochem Sci. 1992. PMID: 1585461 Review.
Cited by
- Aminoacyl tRNA Synthetases: Implications of Structural Biology in Drug Development against Trypanosomatid Parasites.
Nasim F, Qureshi IA. Nasim F, et al. ACS Omega. 2023 Apr 10;8(17):14884-14899. doi: 10.1021/acsomega.3c00826. eCollection 2023 May 2. ACS Omega. 2023. PMID: 37151504 Free PMC article. Review. - Aminoacyl tRNA synthetases as malarial drug targets: a comparative bioinformatics study.
Nyamai DW, Tastan Bishop Ö. Nyamai DW, et al. Malar J. 2019 Feb 6;18(1):34. doi: 10.1186/s12936-019-2665-6. Malar J. 2019. PMID: 30728021 Free PMC article. - Identification and characterization of aspartyl-tRNA synthetase inhibitors against Mycobacterium tuberculosis by an integrated whole-cell target-based approach.
Soto R, Perez-Herran E, Rodriguez B, Duma BM, Cacho-Izquierdo M, Mendoza-Losana A, Lelievre J, Aguirre DB, Ballell L, Cox LR, Alderwick LJ, Besra GS. Soto R, et al. Sci Rep. 2018 Aug 23;8(1):12664. doi: 10.1038/s41598-018-31157-3. Sci Rep. 2018. PMID: 30140040 Free PMC article. - Evolutionary and structural annotation of disease-associated mutations in human aminoacyl-tRNA synthetases.
Datt M, Sharma A. Datt M, et al. BMC Genomics. 2014 Dec 4;15(1):1063. doi: 10.1186/1471-2164-15-1063. BMC Genomics. 2014. PMID: 25476837 Free PMC article. - Identification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.
Ruan ZR, Fang ZP, Ye Q, Lei HY, Eriani G, Zhou XL, Wang ED. Ruan ZR, et al. J Biol Chem. 2015 Jan 16;290(3):1664-78. doi: 10.1074/jbc.M114.599886. Epub 2014 Nov 21. J Biol Chem. 2015. PMID: 25416776 Free PMC article.
References
- Nucleic Acids Res. 1986 Feb 25;14(4):1657-66 - PubMed
- Gene. 1989 Dec 14;84(2):481-5 - PubMed
- J Biol Chem. 1994 Apr 22;269(16):12137-41 - PubMed
- Biochimie. 1993;75(12):1091-8 - PubMed
- Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10816-20 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Molecular Biology Databases