GlyRS mutations in CMT

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Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Dec 1

Crystallization and preliminary X-ray analysis of a native human

tRNA synthetase whose allelic variants are associated with Charcot-

Marie-Tooth disease.

Xie W, Schimmel P, Yang XL.

Department of Molecular Biology, The Skaggs Institute for Chemical

Biology, The Scripps Research Institute, BCC-379, 10550 North Torrey

Pines Road, La Jolla, CA 92037, USA.

Glycyl-tRNA synthetase (GlyRS) is one of a group of enzymes that

catalyze the synthesis of aminoacyl-tRNAs for translation. Mutations

of human and mouse GlyRSs are causally associated with Charcot-Marie-

Tooth disease, the most common genetic disorder of the peripheral

nervous system. As the first step towards a structure-function

analysis of this disease, native human GlyRS was expressed, purified

and crystallized. The crystal belonged to space group P4(3)2(1)2 or

its enantiomorphic space group P4(1)2(1)2, with unit-cell parameters

a = b = 91.74, c = 247.18 A, and diffracted X-rays to 3.0 A

resolution. The asymmetric unit contained one GlyRS molecule and had

a solvent content of 69%.