2Q5H

Crystal structure of apo-wildtype Glycyl-tRNA synthetase

Summary for 2Q5H

• Entry DOI: 10.2210/pdb2q5h/pdb
• Related: 2Q5I
• Descriptor: Glycyl-tRNA synthetase (2 entities in total)
• Functional Keywords: aminoacyl-trna synthetase, atp-binding, structural genomics, glycyl-trna synthetase, oxford protein production facility, oppf, ligase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P41250
• Total number of polymer chains: 1
• Total formula weight: 78462.55

Authors

Cader, M.Z.,Ren, J.,James, P.A.,Bird, L.E.,Talbot, K.,Stammers, D.K.,Oxford Protein Production Facility (OPPF) (deposition date: 2007-06-01, release date: 2007-06-19, Last modification date: 2023-08-30)

Primary citation

Cader, M.Z.,Ren, J.,James, P.A.,Bird, L.E.,Talbot, K.,Stammers, D.K.
Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy.
Febs Lett., 581:2959-2964, 2007

PubMed Abstract: Dominant mutations in the ubiquitous enzyme glycyl-tRNA synthetase (GlyRS), including S581L, lead to motor nerve degeneration. We have determined crystal structures of wildtype and S581L-mutant human GlyRS. The S581L mutation is approximately 50A from the active site, and yet gives reduced aminoacylation activity. The overall structures of wildtype and S581L-GlyRS, including the active site, are very similar. However, residues 567-575 of the anticodon-binding domain shift position and in turn could indirectly affect glycine binding via the tRNA or alternatively inhibit conformational changes. Reduced enzyme activity may underlie neuronal degeneration, although a dominant-negative effect is more likely in this autosomal dominant disorder.

PubMed: 17544401
DOI: 10.1016/j.febslet.2007.05.046

Experimental method

X-RAY DIFFRACTION (3 Å)