3IP4
The high resolution structure of GatCAB
3IP4 の概要
エントリーDOI | 10.2210/pdb3ip4/pdb |
分子名称 | Glutamyl-tRNA(Gln) amidotransferase subunit A, Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B, Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C, ... (5 entities in total) |
機能のキーワード | multi protein complex, ligase, atp-binding, nucleotide-binding, protein biosynthesis |
由来する生物種 | Staphylococcus aureus subsp. aureus 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 118957.08 |
構造登録者 | |
主引用文献 | Nakamura, A.,Sheppard, K.,Yamane, J.,Yao, M.,Soll, D.,Tanaka, I. Two distinct regions in Staphylococcus aureus GatCAB guarantee accurate tRNA recognition Nucleic Acids Res., 38:672-682, 2010 Cited by PubMed Abstract: In many prokaryotes the biosynthesis of the amide aminoacyl-tRNAs, Gln-tRNA(Gln) and Asn-tRNA(Asn), proceeds by an indirect route in which mischarged Glu-tRNA(Gln) or Asp-tRNA(Asn) is amidated to the correct aminoacyl-tRNA catalyzed by a tRNA-dependent amidotransferase (AdT). Two types of AdTs exist: bacteria, archaea and organelles possess heterotrimeric GatCAB, while heterodimeric GatDE occurs exclusively in archaea. Bacterial GatCAB and GatDE recognize the first base pair of the acceptor stem and the D-loop of their tRNA substrates, while archaeal GatCAB recognizes the tertiary core of the tRNA, but not the first base pair. Here, we present the crystal structure of the full-length Staphylococcus aureus GatCAB. Its GatB tail domain possesses a conserved Lys rich motif that is situated close to the variable loop in a GatCAB:tRNA(Gln) docking model. This motif is also conserved in the tail domain of archaeal GatCAB, suggesting this basic region may recognize the tRNA variable loop to discriminate Asp-tRNA(Asn) from Asp-tRNA(Asp) in archaea. Furthermore, we identified a 3(10) turn in GatB that permits the bacterial GatCAB to distinguish a U1-A72 base pair from a G1-C72 pair; the absence of this element in archaeal GatCAB enables the latter enzyme to recognize aminoacyl-tRNAs with G1-C72 base pairs. PubMed: 19906721DOI: 10.1093/nar/gkp955 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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