Publication: Ammonia channel couples glutaminase with transamidase reactions in GatCAB
2
Issued Date
2006-06-30
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ISSN
10959203
00368075
00368075
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2-s2.0-33745596803
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Mahidol University
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SCOPUS
Bibliographic Citation
Science. Vol.312, No.5782 (2006), 1954-1958
Suggested Citation
Akiyoshi Nakamura, Min Yao, Sarin Chimnaronk, Naoki Sakai, Isao Tanaka Ammonia channel couples glutaminase with transamidase reactions in GatCAB. Science. Vol.312, No.5782 (2006), 1954-1958. doi:10.1126/science.1127156 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/23943
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Title
Ammonia channel couples glutaminase with transamidase reactions in GatCAB
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Abstract
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, 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 tRNAGln serve as identity elements essential for discrimination by GatCAB and propose a complete model for the overall concerted reactions to synthesize Gln-tRNAGln.