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Crystal structure of JHP933 form Helicobacter pylori J99 shows twodomain architerture with a DUF 1814 family nucleotidyltransferase domain and a helical bundle domain

Authors
Yoon, Ji YoungLee, Sang JaeKim, Do JinLee, Bong-JinYang, Jin KukSuh, Se Won
Issue Date
Sep-2014
Publisher
WILEY-BLACKWELL
Keywords
Helicolocter pyloric; JHP933; DUF1814; plasticity region; nucletidy
Citation
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.82, no.9, pp.2275 - 2281
Journal Title
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume
82
Number
9
Start Page
2275
End Page
2281
URI
http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/9940
DOI
10.1002/prot.24572
ISSN
0887-3585
Abstract
The jhp0933 gene in the plasticity region of Helicobucter pylori 199 encodes a hypothertical protein (HIP933), which may play some roles in pathogensis. Here we have determined he crystal strutre of JHP933 at 2.17 angstrom. It represent the first crystal strucutre of the DUF1814 protein family. JHP933 consists of two domins and N- termial domain of the nucletidyfrease (NTase fold and a C-terminal helix bondile domain. A highly positively charge surfae patch exists adjecent to the pulative NTP binding site. Strucutal similarity of JHP933 to known NTases is very remote, suggesting that it may function as a novel NTase.
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