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Science 30 June 2006:
Vol. 312. no. 5782, pp. 1954 - 1958
DOI: 10.1126/science.1127156
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Reports

Ammonia Channel Couples Glutaminase with Transamidase Reactions in GatCAB

Akiyoshi Nakamura,1* Min Yao,1* Sarin Chimnaronk,1,2 Naoki Sakai,1 Isao Tanaka1{dagger}

The formation of glutaminyl transfer RNA (Gln-tRNAGln) differs among the three domains of life. Most bacteria employ an indirect pathway to produce Gln-tRNAGln by a heterotrimeric glutamine amidotransferase CAB (GatCAB) that acts on the misacylated Glu-tRNAGln. 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 Å in length. Further, we show that the first U-A base pair in the acceptor stem and the D loop of tRNAGln serve as identity elements essential for discrimination by GatCAB and propose a complete model for the overall concerted reactions to synthesize Gln-tRNAGln.

1 Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.
2 Institute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, Nakornpathom 73170, Thailand.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: tanaka{at}castor.sci.hokudai.ac.jp

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