Backbone NMR assignments of a putative secretory protein from Helicobacter pylori, using a high-field (900 MHz) NMR

Title
Backbone NMR assignments of a putative secretory protein from Helicobacter pylori, using a high-field (900 MHz) NMR
Authors
심대원안희철원형식
Keywords
chemical shift assignment; Helicobacter pylori; HP0902; VacA; Virulence Factor
Issue Date
2009-12
Publisher
Journal of the Korean Magnetic Resonance Society
Citation
VOL 13, NO 2, 108-116
Abstract
The HP0902, a homodimeric 22.1 kDa protein, has been suggested as a putative secretory protein from Helicobacter pylori, although the protein possesses no signal peptide for secretion. Since it may be associated with the virulence of the bacterium, NMR study has been initiated in terms of structural genomics. In our previous effort to assign the backbone NMR resonances, using 800 MHz NMR machine at pH 7.8, the resonances from eight of the 99 residues could not be assined due to missing of the signals. In this work, to enhance the extent of assignments, a 900 MHz machine was employed and the sample pH was reduced down to 6.5. Finally, almost all signals, except for those from G9 and S24, could be clearly assigned. The determined secondary structure using the assined chemical shifts indicated that the HP0902 consists of 11 β-strands with no helices. In our database search result, HP0902 was predicted to interact with VacA (Vacuolating cytotoxin A), which is a representative virulence factor secreted from Helicobacter pylori. Thus, molecular interaction between HP0902 and VacA would be worthy of investigation, on the basis of the present results of NMR assignments.
URI
http://pubs.kist.re.kr/handle/201004/38357
ISSN
1226-6531
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KIST Publication > Article
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