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TitleThe lineage-specific tRNA recognition mechanism of bacterial trptophanyl-tRNA synthetase and its implications for inhibitor discover
Journal, issue, pagesTo Be Published
Publish dateJan 23, 2025 (structure data deposition date)
AuthorsPeng, X. / Xia, K. / Huang, Q. / Xiang, M. / Han, L. / Qiu, H. / Gu, Q. / Chen, B. / Zhou, H.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.59 - 2.82 Å
Structure data

PDB-9lot:
Crystal structure of Escherichia coli trptophanyl-tRNA synthetase in complex with N-piperidine ibrutinib
Method: X-RAY DIFFRACTION / Resolution: 1.59 Å

PDB-9lpc:
Crystal structure of Escherichia coli trptophanyl-tRNA synthetase in complex with tRNA(Trp)
Method: X-RAY DIFFRACTION / Resolution: 2.82 Å

PDB-9lpd:
Crystal structure of Escherichia coli trptophanyl-tRNA synthetase in complex with tirabrutinib
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

PDB-1eky:
MODEL STRUCTURE FROM NON-NOE BASED NMR STRUCTURE CALCULATION

ChemComp-SO4:
SULFATE ION

ChemComp-CLW:
CHLORZOXAZONE

ChemComp-TYM:
TRYPTOPHANYL-5'AMP

ChemComp-HOH:
WATER

PDB-1ek0:
GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION

Source
  • escherichia coli (E. coli)
KeywordsLIGASE / trptophanyl-tRNA synthetase / N-piperidine ibrutinib / complex / LIGASE/RNA / tRNA / LIGASE-RNA complex / trptophayl-tRNA synthetase / Tirabrutinib

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