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- W2090837206 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, Mn 2+ , 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 Å 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 ." @default.
- W2090837206 created "2016-06-24" @default.
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- W2090837206 date "2006-06-30" @default.
- W2090837206 modified "2023-10-02" @default.
- W2090837206 title "Ammonia Channel Couples Glutaminase with Transamidase Reactions in GatCAB" @default.
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- W2090837206 doi "https://doi.org/10.1126/science.1127156" @default.
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