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Peer-reviewedCC BY 4.0Acta Crystallographica Section F: Structural Biology Communications

Crystal structure of tyrosine-tRNA synthetase from Helicobacter pylori G27

  • David Igbalajobi1
  • Jason E. Taylor1
  • Raymond Gao2
  • Jesuferanmi Ayanlade1
  • Rachael Zigweid3,4
  • Sandhya Subramanian3,4
  • Hannah Udell3,4
  • Thomas E. Edwards5
  • Jan Abendroth5
  • Donald Lorimer5
  • Peter J. Myler3,4
  • Bart Staker3,4
2 more authors
  • Edmund Moses Ndip6
  • Oluwatoyin A. Asojo4,7,8
8 affiliations
  1. 1Dartmouth College Hanover New Hampshire USA
  2. 2University of California, Berkeley, Berkeley, California, USA
  3. 3Center for Global Infectious Disease Research Seattle Children’s Research Institute 307 Westlake Avenue North, Suite 500 Seattle WA 98109 USA
  4. 4Seattle Structural Genomics Center for Infectious Diseases, Seattle, Washington, USA
  5. 5UCB BioSciences, Bainbridge Island, Washington, USA
  6. 6Chemistry and Biochemistry Hampton University Hampton VA 23666 USA
  7. 7Dartmouth Cancer Center, Lebanon, New Hampshire, USA
  8. 8Biochemistry and Cell Biology, Dartmouth Geisel School of Medicine, New Hampshire, USA
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Abstract

Helicobacter pylori, a major cause of gastric ulcers and cancers, infects nearly half of the world’s population. The crystal structure of a potential H. pylori structure-guided drug-discovery target, tyrosine-tRNA synthetase (HpTyrRS), has been determined by the Seattle Structural Genomics Center for Infectious Disease (SSGCID). HpTyrRS is an enzyme that catalyzes the ATP-dependent attachment of tyrosine to tRNA. HpTyrRS was produced and crystallized, and its structure was determined at 2.2 Å resolution. HpTyrRS has a prototypical bacterial TyrRS topology and forms dimers in solution. HpTyrRS shares a conserved binding cavity for a previously identified Staphylococcus aureus TyrRS inhibitor (SB-219383). The reported structure and analysis establish HpTyrRS as a potential target for structure-guided drug discovery and repurposing.

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Cite

BibTeXRIS
BibTeX
@article{igbalajobi2026crystal,
  title = {{Crystal structure of tyrosine-tRNA synthetase from Helicobacter pylori G27}},
  author = {David Igbalajobi and Jason E. Taylor and Raymond Gao and Jesuferanmi Ayanlade and Rachael Zigweid and Sandhya Subramanian and Hannah Udell and Thomas E. Edwards and Jan Abendroth and Donald Lorimer and Peter J. Myler and Bart Staker and Edmund Moses Ndip and Oluwatoyin A. Asojo},
  journal = {Acta Crystallographica Section F: Structural Biology Communications},
  year = {2026},
  month = oct,
  doi = {10.1107/s2053230x26010253},
  url = {https://doi.org/10.1107/s2053230x26010253},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Crystal structure of tyrosine-tRNA synthetase from Helicobacter pylori G27
AU  - David Igbalajobi
AU  - Jason E. Taylor
AU  - Raymond Gao
AU  - Jesuferanmi Ayanlade
AU  - Rachael Zigweid
AU  - Sandhya Subramanian
AU  - Hannah Udell
AU  - Thomas E. Edwards
AU  - Jan Abendroth
AU  - Donald Lorimer
AU  - Peter J. Myler
AU  - Bart Staker
AU  - Edmund Moses Ndip
AU  - Oluwatoyin A. Asojo
PY  - 2026
DA  - 2026/10/23
JO  - Acta Crystallographica Section F: Structural Biology Communications
DO  - 10.1107/s2053230x26010253
UR  - https://doi.org/10.1107/s2053230x26010253
AB  - Helicobacter pylori, a major cause of gastric ulcers and cancers, infects nearly half of the world’s population. The crystal structure of a potential H. pylori structure-guided drug-discovery target, tyrosine-tRNA synthetase (HpTyrRS), has been determined by the Seattle Structural Genomics Center for Infectious Disease (SSGCID). HpTyrRS is an enzyme that catalyzes the ATP-dependent attachment of tyrosine to tRNA. HpTyrRS was produced and crystallized, and its structure was determined at 2.2 Å resolution. HpTyrRS has a prototypical bacterial TyrRS topology and forms dimers in solution. HpTyrRS shares a conserved binding cavity for a previously identified Staphylococcus aureus TyrRS inhibitor (SB-219383). The reported structure and analysis establish HpTyrRS as a potential target for structure-guided drug discovery and repurposing.
SN  - 2053-230X
ER  -