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A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases.
Biochimie. 1995; 77(3):194-203.B

Abstract

The superimposable dinucleotide fold domains of MetRS, GlnRS and TyrRS define structurally equivalent amino acids which have been used to constrain the sequence alignments of the 10 class I aminoacyl-tRNA synthetases (aaRS). The conservation of those residues which have been shown to be critical in some aaRS enables to predict their location and function in the other synthetases, particularly: i) a conserved negatively-charged residue which binds the alpha-amino group of the amino acid substrate; ii) conserved residues within the inserted domain bridging the two halves of the dinucleotide-binding fold; and iii) conserved residues in the second half of the fold which bind the amino acid and ATP substrate. The alignments also indicate that the class I synthetases may be partitioned into two subgroups: a) MetRS, IleRS, LeuRS, ValRS, CysRS and ArgRS; b) GlnRS, GluRS, TyrRS and TrpRS.

Authors+Show Affiliations

Centre de Génétique Moléculaire, Université P & M Curie, Gif-sur-Yvette, France.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7647112

Citation

Landès, C, et al. "A Structure-based Multiple Sequence Alignment of All Class I aminoacyl-tRNA Synthetases." Biochimie, vol. 77, no. 3, 1995, pp. 194-203.
Landès C, Perona JJ, Brunie S, et al. A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases. Biochimie. 1995;77(3):194-203.
Landès, C., Perona, J. J., Brunie, S., Rould, M. A., Zelwer, C., Steitz, T. A., & Risler, J. L. (1995). A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases. Biochimie, 77(3), 194-203.
Landès C, et al. A Structure-based Multiple Sequence Alignment of All Class I aminoacyl-tRNA Synthetases. Biochimie. 1995;77(3):194-203. PubMed PMID: 7647112.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases. AU - Landès,C, AU - Perona,J J, AU - Brunie,S, AU - Rould,M A, AU - Zelwer,C, AU - Steitz,T A, AU - Risler,J L, PY - 1995/1/1/pubmed PY - 1995/1/1/medline PY - 1995/1/1/entrez SP - 194 EP - 203 JF - Biochimie JO - Biochimie VL - 77 IS - 3 N2 - The superimposable dinucleotide fold domains of MetRS, GlnRS and TyrRS define structurally equivalent amino acids which have been used to constrain the sequence alignments of the 10 class I aminoacyl-tRNA synthetases (aaRS). The conservation of those residues which have been shown to be critical in some aaRS enables to predict their location and function in the other synthetases, particularly: i) a conserved negatively-charged residue which binds the alpha-amino group of the amino acid substrate; ii) conserved residues within the inserted domain bridging the two halves of the dinucleotide-binding fold; and iii) conserved residues in the second half of the fold which bind the amino acid and ATP substrate. The alignments also indicate that the class I synthetases may be partitioned into two subgroups: a) MetRS, IleRS, LeuRS, ValRS, CysRS and ArgRS; b) GlnRS, GluRS, TyrRS and TrpRS. SN - 0300-9084 UR - https://www.unboundmedicine.com/medline/citation/7647112/A_structure_based_multiple_sequence_alignment_of_all_class_I_aminoacyl_tRNA_synthetases_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0300-9084(96)88125-9 DB - PRIME DP - Unbound Medicine ER -