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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

Kim MK
Department of Life Science, Kwangju Institute of Science and Technology, Gwangju 500-712, Korea.
Song HE
No affiliation info available
Kim YS
No affiliation info available
Rho SH
No affiliation info available
Im YJ
No affiliation info available
Lee JH
No affiliation info available
Kang GB
No affiliation info available
Eom SH
No affiliation info available

MeSH

CrystallizationCrystallography, X-RayEscherichia coliHelicobacter pyloriOrotate PhosphoribosyltransferaseProtein ConformationSalmonella typhimuriumSequence AlignmentTransfection

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 -