3lw3
From Proteopedia
Crystal structure of HP0420-homologue from Helicobacter felis
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHelicobacter 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. References
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