2q5h

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spinqualitylabelsall models 2q5h, resolution 3.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of apo-wildtype Glycyl-tRNA synthetase

Overview

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.

About this Structure

2Q5H is a Single protein structure of sequence from Homo sapiens. Active as Glycine--tRNA ligase, with EC number 6.1.1.14 Full crystallographic information is available from OCA.

Reference

Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy., Cader MZ, Ren J, James PA, Bird LE, Talbot K, Stammers DK, FEBS Lett. 2007 Jun 26;581(16):2959-2964. Epub 2007 May 29. PMID:17544401

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