Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus

Logan, D. T. LU orcid ; Mazauric, M.-H. ; Kern, D. and Moras, D. (1995) In EMBO Journal 14(17). p.4156-4167
Abstract

The sequence and crystal structure at 2.75 Å resolution of the homodimeric glycyl-tRNA synthetase from Thermus thermophilus, the first representative of the last unknown class II synthetase subgroup, have been determined. The three class II synthetase sequence motifs are present but the structure was essential for identification of motif 1, which does not possess the proline previously believed to be an essential class II invariant. Nevertheless, crucial contacts with the active site of the other monomer involving motif 1 are conserved and a more comprehensive description of class II now becomes possible. Each monomer consists of an active site strongly resembling that of the aspartyl and seryl enzymes, a C-terminal anticodon... (More)

The sequence and crystal structure at 2.75 Å resolution of the homodimeric glycyl-tRNA synthetase from Thermus thermophilus, the first representative of the last unknown class II synthetase subgroup, have been determined. The three class II synthetase sequence motifs are present but the structure was essential for identification of motif 1, which does not possess the proline previously believed to be an essential class II invariant. Nevertheless, crucial contacts with the active site of the other monomer involving motif 1 are conserved and a more comprehensive description of class II now becomes possible. Each monomer consists of an active site strongly resembling that of the aspartyl and seryl enzymes, a C-terminal anticodon recognition domain of 100 residues and a third domain unusually inserted between motifs 1 and 2 almost certainly interacting with the acceptor arm of tRNA(Gly). The C-terminal domain has a novel five-stranded parallel-antiparallel β-sheet structure with three surrounding helices. The active site residues most probably responsible for substrate recognition, in particular in the Gly binding pocket, can be identified by inference from aspartyl-tRNA synthetase due to the conserved nature of the class II active site.

(Less)
Please use this url to cite or link to this publication:
author
; ; and
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Crystal structure, Glycyl-tRNA synthetase, Prokaryote, Sequence motifs, Substrate modelling
in
EMBO Journal
volume
14
issue
17
pages
12 pages
publisher
Oxford University Press
external identifiers
  • pmid:7556056
  • scopus:0029091055
ISSN
0261-4189
DOI
10.1002/j.1460-2075.1995.tb00089.x
language
English
LU publication?
no
id
1cce0d15-c718-49c3-b622-a87db7bd661e
date added to LUP
2022-04-25 11:32:21
date last changed
2024-05-31 15:01:04
@article{1cce0d15-c718-49c3-b622-a87db7bd661e,
  abstract     = {{<p>The sequence and crystal structure at 2.75 Å resolution of the homodimeric glycyl-tRNA synthetase from Thermus thermophilus, the first representative of the last unknown class II synthetase subgroup, have been determined. The three class II synthetase sequence motifs are present but the structure was essential for identification of motif 1, which does not possess the proline previously believed to be an essential class II invariant. Nevertheless, crucial contacts with the active site of the other monomer involving motif 1 are conserved and a more comprehensive description of class II now becomes possible. Each monomer consists of an active site strongly resembling that of the aspartyl and seryl enzymes, a C-terminal anticodon recognition domain of 100 residues and a third domain unusually inserted between motifs 1 and 2 almost certainly interacting with the acceptor arm of tRNA(Gly). The C-terminal domain has a novel five-stranded parallel-antiparallel β-sheet structure with three surrounding helices. The active site residues most probably responsible for substrate recognition, in particular in the Gly binding pocket, can be identified by inference from aspartyl-tRNA synthetase due to the conserved nature of the class II active site.</p>}},
  author       = {{Logan, D. T. and Mazauric, M.-H. and Kern, D. and Moras, D.}},
  issn         = {{0261-4189}},
  keywords     = {{Crystal structure; Glycyl-tRNA synthetase; Prokaryote; Sequence motifs; Substrate modelling}},
  language     = {{eng}},
  number       = {{17}},
  pages        = {{4156--4167}},
  publisher    = {{Oxford University Press}},
  series       = {{EMBO Journal}},
  title        = {{Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus}},
  url          = {{http://dx.doi.org/10.1002/j.1460-2075.1995.tb00089.x}},
  doi          = {{10.1002/j.1460-2075.1995.tb00089.x}},
  volume       = {{14}},
  year         = {{1995}},
}