Crystal structure and functional insight of HP0420-homolog from Helicobacter felis

Shunfu Piao, Xiao Ling Jin, Bo Young Yun, Nahee Kim, Hyun Soo Cho, Minoru Fukuda, Heeseob Lee, Nam Chul Ha

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


Helicobacter pylori infect more than half of the world's population and are considered a cause of peptic ulcer disease and gastric cancer. Recently, hypothetical gene HP0421 was identified in H. pylori as a cholesterol α-glucosyltransferase, which is required to synthesize cholesteryl glucosides, essential cell wall components of the bacteria. In the same gene-cluster, HP0420 was co-identified, whose function remains unknown. Here we report the crystal structure of HP0420-homolog of H. felis (HF0420) to gain insight into the function of HP0420. The crystal structure, combined with size-exclusion chromatography, reveals that HF0420 adopts a homodimeric hot-dog fold. The crystal structure suggests that HF0420 has enzymatic activity that involves a conserved histidine residue at the end of the central α-helix. Subsequent biochemical studies provide clues to the function of HP0420 and HF0420.

Original languageEnglish
Pages (from-to)940-946
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - 2010 Apr 16

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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