Ammonia channel couples glutaminase with transamidase reactions in GatCAB.

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Nakamura A, Yao M, Chimnaronk S, Sakai N, Tanaka I

Ammonia channel couples glutaminase with transamidase reactions in GatCAB.

Science. 2006 Jun 30;312(5782):1954-8.

PubMed ID

16809541 [ View in PubMed

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Abstract

The formation of glutaminyl transfer RNA (Gln-tRNA(Gln)) differs among the three domains of life. Most bacteria employ an indirect pathway to produce Gln-tRNA(Gln) by a heterotrimeric glutamine amidotransferase CAB (GatCAB) that acts on the misacylated Glu-tRNA(Gln). Here, we describe a series of crystal structures of intact GatCAB from Staphylococcus aureus in the apo form and in the complexes with glutamine, asparagine, Mn2+, and adenosine triphosphate analog. Two identified catalytic centers for the glutaminase and transamidase reactions are markedly distant but connected by a hydrophilic ammonia channel 30 A in length. Further, we show that the first U-A base pair in the acceptor stem and the D loop of tRNA(Gln) serve as identity elements essential for discrimination by GatCAB and propose a complete model for the overall concerted reactions to synthesize Gln-tRNA(Gln).

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
L-Glutamine	GMP synthase [glutamine-hydrolyzing]	Protein	Humans	Unknown	Substrate	Details