Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase-Reference-Cited by-同舟云学术

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Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase

Published:2010-03-15 Issue:4 Volume:29 Page:397-405
ISSN:1016-8478
Container-title:Molecules and Cells
language:en
Short-container-title:Mol Cells

Author:

Kim Hun,Choi Jongkeun,Kim Truc,Lokanath Neratur K.,Ha Sung Chul,Suh Se Won,Hwang Hye-Yeon,Kim Kyeong Kyu

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/s10059-010-0047-6.pdf

Reference25 articles.

1. Aragao, D., Fialho, A.M., Marques, A.R., Mitchell, E.P., Sa-Correia, I., and Frazao, C. (2007). The complex of Sphingomonas elodea ATCC 31461 glucose-1-phosphate uridylyltransferase with glucose-1-phosphate reveals a novel quaternary structure, unique among nucleoside diphosphate-sugar pyrophosphorylase members. J. Bacteriol. 189, 4520–4528.

2. Blankenfeldt, W., Asuncion, M., Lam, J., and Naismith, J. (2000). The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA). EMBO J. 19, 6652–6663.

3. Brünger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. (1998). Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905–921.

4. Chang, H.Y., Lee, J.H., Deng, W.L., Fu, T.F., and Peng, H.L. (1996). Virulence and outer membrane properties of a galU mutant of Klebsiella pneumoniae CG43. Microb. Pathog. 20, 255–261.

5. Clatworthy, A.E., Pierson, E., and Hung, D.T. (2007). Targeting virulence: a new paradigm for antimicrobial therapy. Nat. Chem. Biol. 3, 541–548.

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