Literature DB >> 3546298

Crystallization and preliminary X-ray investigation of uridine phosphorylase from Escherichia coli.

W J Cook, G W Koszalka, W W Hall, S V Narayana, S E Ealick.   

Abstract

Crystals of uridine phosphorylase from Escherichia coli K12 have been grown from solutions of polyethylene glycol 4000. The crystals are trigonal, space group R3; the hexagonal axes are a = 154.4 A and c = 49.4 A. The crystals are quite stable to x-rays and diffract beyond 2.6 A resolution. It appears that the molecule is a hexamer with a subunit molecular weight of 27,500 and utilizes the 3-fold symmetry of the space group, resulting in two subunits/asymmetric unit.

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Year:  1987        PMID： 3546298

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  3 in total

1.  Modification of uridine phosphorylase from Escherichia coli by diethyl pyrocarbonate. Evidence for a histidine residue in the active site of the enzyme.

Authors:  A K Drabikowska; G Woźniak
Journal:  Biochem J       Date:  1990-09-01       Impact factor: 3.857

2.  Nucleotide sequence of the Escherichia coli uridine phosphorylase (udp) gene.

Authors:  L Walton; C A Richards; L P Elwell
Journal:  Nucleic Acids Res       Date:  1989-08-25       Impact factor: 16.971

3.  Purification and characterization of the hydantoin racemase of Pseudomonas sp. strain NS671 expressed in Escherichia coli.

Authors:  K Watabe; T Ishikawa; Y Mukohara; H Nakamura
Journal:  J Bacteriol       Date:  1992-12       Impact factor: 3.490
  3 in total

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