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 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 language | English |
|---|---|
| Pages (from-to) | 940-946 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 394 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2010 Apr 16 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Crystal structure and functional insight of HP0420-homolog from Helicobacter felis. / Piao, Shunfu; Jin, Xiao Ling; Yun, Bo Young; Kim, Nahee; Cho, Hyun Soo; Fukuda, Minoru; Lee, Heeseob; Ha, Nam Chul.
In: Biochemical and Biophysical Research Communications, Vol. 394, No. 4, 16.04.2010, p. 940-946.Research output: Contribution to journal › Article
TY - JOUR
T1 - Crystal structure and functional insight of HP0420-homolog from Helicobacter felis
AU - Piao, Shunfu
AU - Jin, Xiao Ling
AU - Yun, Bo Young
AU - Kim, Nahee
AU - Cho, Hyun Soo
AU - Fukuda, Minoru
AU - Lee, Heeseob
AU - Ha, Nam Chul
PY - 2010/4/16
Y1 - 2010/4/16
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77950865071&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77950865071&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2010.03.087
DO - 10.1016/j.bbrc.2010.03.087
M3 - Article
C2 - 20302842
AN - SCOPUS:77950865071
VL - 394
SP - 940
EP - 946
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -