2DQN
Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Asn
Summary for 2DQN
| Entry DOI | 10.2210/pdb2dqn/pdb |
| Related | 2DF4 2F2A 2G5H 2G5I |
| Descriptor | Glutamyl-tRNA(Gln) amidotransferase subunit A, Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B, Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C, ... (6 entities in total) |
| Functional Keywords | trna, amidotransferase, ligase |
| Biological source | Staphylococcus aureus More |
| Total number of polymer chains | 3 |
| Total formula weight | 119089.20 |
| Authors | Nakamura, A.,Yao, M.,Tanaka, I. (deposition date: 2006-05-29, release date: 2006-07-18, Last modification date: 2023-10-25) |
| Primary citation | Nakamura, A.,Yao, M.,Chimnaronk, S.,Sakai, N.,Tanaka, I. Ammonia channel couples glutaminase with transamidase reactions in GatCAB Science, 312:1954-1958, 2006 Cited by PubMed 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). PubMed: 16809541DOI: 10.1126/science.1127156 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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