OAK

Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori

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Author(s)
Kim, MKSong, HEKim, YSRho, SHIm, YJLee, JHKang, GBEom, Soo Hyun
Type
Article
Citation
Molecules and Cells, v.15, no.3, pp.361 - 363
Issued Date
2003-06
Abstract
Orotic acid phosphoribosyltransferase (PyrE) (EC 2.4.2.10) is a key enzyme in de novo uridine monophosphate (UMP) biosynthesis. It catalyzes the reaction between orotic acid and 5-phosphoribosyl-1-pyrophosphate (PRPP) to yield orotidine monophosphate (OMP), which is transformed to uridine monophosphate by decarboxylation. H. pylori PyrE was crystallized at 294 +/- 1 K by the hanging drop vapor-diffusion method. The crystals belong to the space group P2(1)2(1)2(1) with unit-cell dimensions a = 95.8, b = 104.9, c = 281.1 Angstrom, alpha = beta = gamma = 90degrees. A set of diffraction data was collected to 3.29 Angstrom resolution using synchrotron X-ray radiation.
Publisher
SPRINGER-VERLAG SINGAPORE PTE LTD
ISSN
1016-8478
DOI
10.1016/S0925-3467(02)00370-1
URI
https://scholar.gist.ac.kr/handle/local/18357
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