Crystal structure and functional insight of HP0420-homolog from Helicobacter felis.
Crystal structure and functional insight of HP0420-homolog from Helicobacter felis.
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DOI:
10.1016/j.bbrc.2010.03.087
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发表时间:
2010-04-16
影响因子:
3.1
通讯作者:
Ha, Nam-Chul
中科院分区:
文献类型:
--
作者:
Piao, Shunfu;Jin, Xiao Ling;Yun, Bo-Young;Kim, Nahee;Cho, Hyun-Soo;Fukuda, Minoru;Lee, Heeseob;Ha, Nam-Chul
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.
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