Literature DB >> 15272173

Crystallization and preliminary X-ray crystallographic study of UDP-glucose pyrophosphorylase (UGPase) from Helicobacter pylori.

Hun Kim1, Chun Ai Wu, Dong Young Kim, Young-Hyun Han, Sung Chul Ha, Chun-Sang Kim, Se Won Suh, Kyeong Kyu Kim.   

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.

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Year:  2004        PMID: 15272173     DOI: 10.1107/S0907444904012727

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  3 in total

Review 1.  The structural biology of enzymes involved in natural product glycosylation.

Authors:  Shanteri Singh; George N Phillips; Jon S Thorson
Journal:  Nat Prod Rep       Date:  2012-06-12       Impact factor: 13.423

2.  Cloning, expression, purification, crystallization and preliminary structure determination of glucose-1-phosphate uridylyltransferase (UgpG) from Sphingomonas elodea ATCC 31461 bound to glucose-1-phosphate.

Authors:  D Aragão; A R Marques; C Frazão; F J Enguita; M A Carrondo; A M Fialho; I Sá-Correia; E P Mitchell
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-08-26

3.  The molecular architecture of glucose-1-phosphate uridylyltransferase.

Authors:  James B Thoden; Hazel M Holden
Journal:  Protein Sci       Date:  2007-03       Impact factor: 6.725

  3 in total

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