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Structure paper

TitleThe binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements.
Journal, issue, pagesSci Adv, Vol. 9, Page eadf1027-eadf1027, Year 2023
Publish dateAug 12, 2022 (structure data deposition date)
AuthorsHan, L. / Luo, Z. / Ju, Y. / Chen, B. / Zou, T. / Wang, J. / Xu, J. / Gu, Q. / Yang, X.L. / Schimmel, P. / Zhou, H.
External linksSci Adv / PubMed:36753552
MethodsX-ray diffraction
Resolution2.907 Å
Structure data

PDB-7yse:
Crystal structure of E. coli heterotetrameric GlyRS in complex with tRNA
Method: X-RAY DIFFRACTION / Resolution: 2.907 Å

Chemicals

ChemComp-JPO:
[(2R,3S,4R,5R)-5-(6-azanyl-2-chloranyl-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-(2-azanylethanoyl)sulfamate

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli (E. coli)
KeywordsTRANSFERASE/RNA / aminoacyl-tRNA synthetase / hetertetramer / drug target / protein-tRNA complex / TRANSFERASE / TRANSFERASE-RNA complex

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