3LW3

Crystal structure of HP0420-homologue from Helicobacter felis

Summary for 3LW3

• Entry DOI: 10.2210/pdb3lw3/pdb
• Related: 3LWG
• Descriptor: HP0420 homologue (2 entities in total)
• Functional Keywords: helicobacter, hotdog-fold, structural genomics, unknown function
• Biological source: Helicobacter felis
• Total number of polymer chains: 2
• Total formula weight: 32197.38

Authors

Ha, N.-C.,Piao, S. (deposition date: 2010-02-23, release date: 2010-04-07, Last modification date: 2023-11-01)

Primary citation

Piao, S.,Jin, X.L.,Yun, B.-Y.,Kim, N.,Cho, H.-S.,Fukuda, M.,Lee, H.,Ha, N.-C.
Crystal structure and functional insight of HP0420-homolog from Helicobacter felis
Biochem.Biophys.Res.Commun., 394:940-946, 2010

PubMed Abstract: 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.

PubMed: 20302842
DOI: 10.1016/j.bbrc.2010.03.087

Experimental method

X-RAY DIFFRACTION (1.6 Å)