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3WQY

Crystal structure of Archaeoglobus fulgidus alanyl-tRNA synthetase in complex with wild-type tRNA(Ala) having G3.U70

Summary for 3WQY
Entry DOI10.2210/pdb3wqy/pdb
Related3WQZ
DescriptorAlanine--tRNA ligase, RNA (75-MER), '5'-O-(N-(L-ALANYL)-SULFAMOYL)ADENOSINE, ... (5 entities in total)
Functional Keywordsaminoacyl-trna synthetases, protein-rna complex, ligase, alanyladenylate analogue, ligase-rna complex, ligase/rna
Biological sourceArchaeoglobus fulgidus
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Cellular locationCytoplasm (By similarity): O28029
Total number of polymer chains3
Total formula weight230529.31
Authors
Naganuma, M.,Sekine, S.,Yokoyama, S. (deposition date: 2014-02-05, release date: 2014-06-18, Last modification date: 2024-03-20)
Primary citationNaganuma, M.,Sekine, S.,Chong, Y.E.,Guo, M.,Yang, X.L.,Gamper, H.,Hou, Y.M.,Schimmel, P.,Yokoyama, S.
The selective tRNA aminoacylation mechanism based on a single G.U pair
Nature, 510:507-511, 2014
Cited by
PubMed Abstract: Ligation of tRNAs with their cognate amino acids, by aminoacyl-tRNA synthetases, establishes the genetic code. Throughout evolution, tRNA(Ala) selection by alanyl-tRNA synthetase (AlaRS) has depended predominantly on a single wobble base pair in the acceptor stem, G3•U70, mainly on the kcat level. Here we report the crystal structures of an archaeal AlaRS in complex with tRNA(Ala) with G3•U70 and its A3•U70 variant. AlaRS interacts with both the minor- and the major-groove sides of G3•U70, widening the major groove. The geometry difference between G3•U70 and A3•U70 is transmitted along the acceptor stem to the 3'-CCA region. Thus, the 3'-CCA region of tRNA(Ala) with G3•U70 is oriented to the reactive route that reaches the active site, whereas that of the A3•U70 variant is folded back into the non-reactive route. This novel mechanism enables the single wobble pair to dominantly determine the specificity of tRNA selection, by an approximate 100-fold difference in kcat.
PubMed: 24919148
DOI: 10.1038/nature13440
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.3 Å)
Structure validation

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