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Crystallization and preliminary X-ray crystallographic study of UDP-glucose pyrophosphorylase (UGPase) from Helicobacter pylori.
Acta Crystallogr D Biol Crystallogr. 2004 Aug; 60(Pt 8):1447-9.AC

Abstract

UDP-glucose pyrophosphorylase (UGPase) catalyzes the synthesis of UDP-glucose, an essential metabolite in all living organisms. An X-ray crystallographic study of UGPase from Helicobacter pylori has been performed in order to elucidate its role in the regulation of this important metabolic pathway. UGPase was crystallized from 0.1 M sodium acetate trihydrate pH 4.6, 2.0 M ammonium sulfate and 0.1 M guanidine-HCl. According to diffraction data collected at a resolution of 2.9 A using a synchrotron-radiation source, the crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 91.47, b = 98.61, c = 245.70 A, alpha = beta = gamma = 90.0 degrees.

Authors+Show Affiliations

Department of Molecular Cell Biology, Center for Molecular Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, South 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)

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

Language

eng

PubMed ID

15272173

Citation

Kim, Hun, et al. "Crystallization and Preliminary X-ray Crystallographic Study of UDP-glucose Pyrophosphorylase (UGPase) From Helicobacter Pylori." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 8, 2004, pp. 1447-9.
Kim H, Wu CA, Kim DY, et al. Crystallization and preliminary X-ray crystallographic study of UDP-glucose pyrophosphorylase (UGPase) from Helicobacter pylori. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 8):1447-9.
Kim, H., Wu, C. A., Kim, D. Y., Han, Y. H., Ha, S. C., Kim, C. S., Suh, S. W., & Kim, K. K. (2004). Crystallization and preliminary X-ray crystallographic study of UDP-glucose pyrophosphorylase (UGPase) from Helicobacter pylori. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 8), 1447-9.
Kim H, et al. Crystallization and Preliminary X-ray Crystallographic Study of UDP-glucose Pyrophosphorylase (UGPase) From Helicobacter Pylori. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 8):1447-9. PubMed PMID: 15272173.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic study of UDP-glucose pyrophosphorylase (UGPase) from Helicobacter pylori. AU - Kim,Hun, AU - Wu,Chun Ai, AU - Kim,Dong Young, AU - Han,Young-Hyun, AU - Ha,Sung Chul, AU - Kim,Chun-Sang, AU - Suh,Se Won, AU - Kim,Kyeong Kyu, Y1 - 2004/07/21/ PY - 2004/01/12/received PY - 2004/05/25/accepted PY - 2004/7/24/pubmed PY - 2005/2/19/medline PY - 2004/7/24/entrez SP - 1447 EP - 9 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 8 N2 - UDP-glucose pyrophosphorylase (UGPase) catalyzes the synthesis of UDP-glucose, an essential metabolite in all living organisms. An X-ray crystallographic study of UGPase from Helicobacter pylori has been performed in order to elucidate its role in the regulation of this important metabolic pathway. UGPase was crystallized from 0.1 M sodium acetate trihydrate pH 4.6, 2.0 M ammonium sulfate and 0.1 M guanidine-HCl. According to diffraction data collected at a resolution of 2.9 A using a synchrotron-radiation source, the crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 91.47, b = 98.61, c = 245.70 A, alpha = beta = gamma = 90.0 degrees. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15272173/Crystallization_and_preliminary_X_ray_crystallographic_study_of_UDP_glucose_pyrophosphorylase__UGPase__from_Helicobacter_pylori_ DB - PRIME DP - Unbound Medicine ER -