Literature DB >> 1518057

Crystallization and preliminary crystallographic studies of glucosamine-6-phosphate deaminase from Escherichia coli K12.

E Horjales1, M M Altamirano, M L Calcagno, Z Dauter, K Wilson, R C Garratt, G Oliva.   

Abstract

Hexameric glucosamine-6-phosphate deaminase from Escherichia coli has been crystallized isomorphously with both phosphate and ammonium sulphate as precipitants, over a wide pH range (6.0 to 9.0). The crystals belong to space group R32 and the cell parameters in the hexagonal setting are a = b = 125.9 A and c = 223.2 A. A complete native data set was collected to 2.1 A resolution. Self-rotation function studies suggest that the hexamers sit on the 3-fold axis and have point group symmetry 32, with a non-crystallographic dyad relating two monomers linked by an interchain disulfide bridge. A possible packing for the unit cell is proposed.

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Year:  1992        PMID: 1518057     DOI: 10.1016/0022-2836(92)91068-z

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  3 in total

1.  Coordinated regulation of amino sugar-synthesizing and -degrading enzymes in Escherichia coli K-12.

Authors:  J A Plumbridge; O Cochet; J M Souza; M M Altamirano; M L Calcagno; B Badet
Journal:  J Bacteriol       Date:  1993-08       Impact factor: 3.490

2.  Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides.

Authors:  M M Altamirano; J A Plumbridge; H A Barba; M L Calcagno
Journal:  Biochem J       Date:  1993-11-01       Impact factor: 3.857

3.  Heterogeneity of quaternary structure of glucosamine-6-phosphate deaminase from Giardia lamblia.

Authors:  Karolina Kwiatkowska-Semrau; Justyna Czarnecka; Marek Wojciechowski; Sławomir Milewski
Journal:  Parasitol Res       Date:  2014-10-19       Impact factor: 2.289

  3 in total

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