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 Young; Lee, Sang Jae; Kim, Do Jin; Lee, Bong-Jin; Yang, Jin Kuk; Suh, 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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Collections - College of Natural Sciences > Department of Chemistry > 1. Journal Articles
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