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Overview
Glutaminyl-tRNA synthetase or GlnRS is a class 1 tRNA synthetase that requires tRNA binding for adenylate synthesis, which suggests that the large substrate could be required to form the active site structure. [3] Genetic evidence shows that induced fit conformational changes are a big part in the mechanism of GlnRS. [3] Glutaminyl-tRNA synthetase is an enzyme which is able to catalyze the transfer of the amino acid glutamine to the A76 hydroxyl group of tRNA^Gln. [3]
Structure
The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase at 2.4 A shows substrate binding is needed to construct a catalytically proficient active site. [3] The backbone atoms of 94 amino acid residues, could be superimposed on their counterparts showing similarities close to each other. [3] One of the amino acids in the of the dinucleotide fold adopts a new arrangement in the unligand enzyme. [3]
Mutations
Mutations in the coding of glutaminyl-tRNA synthetase can cause seizures especially in infants. [4] Progressive microcephaly is a condition that involves mutations in gene coding of brain survival. [4]
Structural highlights
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