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Publication Abstract from PubMed

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 alpha-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 alpha-helix. Subsequent biochemical studies provide clues to the function of HP0420 and HF0420.

Crystal structure and functional insight of HP0420-homolog from Helicobacter felis.,Piao S, Jin XL, Yun BY, Kim N, Cho HS, Fukuda M, Lee H, Ha NC Biochem Biophys Res Commun. 2010 Apr 16;394(4):940-6. Epub 2010 Mar 17. PMID:20302842^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.