Tags

Type your tag names separated by a space and hit enter

Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori.
Mol Cells. 2003 Jun 30; 15(3):361-3.MC

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 A, alpha = beta = gamma = 90 degrees. A set of diffraction data was collected to 3.29 A resolution using synchrotron X-ray radiation.

Authors+Show Affiliations

Department of Life Science, Kwangju Institute of Science and Technology, Gwangju 500-712, Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12872993

Citation

Kim, Mun-Kyoung, et al. "Crystallization and Preliminary X-ray Crystallographic Analysis of Orotate Phosphoribosyltransferase From Helicobacter Pylori." Molecules and Cells, vol. 15, no. 3, 2003, pp. 361-3.
Kim MK, Song HE, Kim YS, et al. Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori. Mol Cells. 2003;15(3):361-3.
Kim, M. K., Song, H. E., Kim, Y. S., Rho, S. H., Im, Y. J., Lee, J. H., Kang, G. B., & Eom, S. H. (2003). Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori. Molecules and Cells, 15(3), 361-3.
Kim MK, et al. Crystallization and Preliminary X-ray Crystallographic Analysis of Orotate Phosphoribosyltransferase From Helicobacter Pylori. Mol Cells. 2003 Jun 30;15(3):361-3. PubMed PMID: 12872993.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori. AU - Kim,Mun-Kyoung, AU - Song,Hye-Eun, AU - Kim,Yun Sik, AU - Rho,Seong-Hwan, AU - Im,Young Jun, AU - Lee,Jun Hyuck, AU - Kang,Gil Bu, AU - Eom,Soo Hyun, PY - 2003/7/23/pubmed PY - 2004/4/13/medline PY - 2003/7/23/entrez SP - 361 EP - 3 JF - Molecules and cells JO - Mol Cells VL - 15 IS - 3 N2 - 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 A, alpha = beta = gamma = 90 degrees. A set of diffraction data was collected to 3.29 A resolution using synchrotron X-ray radiation. SN - 1016-8478 UR - https://www.unboundmedicine.com/medline/citation/12872993/Crystallization_and_preliminary_X_ray_crystallographic_analysis_of_orotate_phosphoribosyltransferase_from_Helicobacter_pylori_ DB - PRIME DP - Unbound Medicine ER -