Literature DB >> 1942042

Crystallization and crystal packing of Proteus mirabilis PR catalase.

H M Jouve1, P Gouet, N Boudjada, G Buisson, R Kahn, E Duee.   

Abstract

The tetrameric catalase from Proteus mirabilis PR (EC 1.11.1.6), known to bind NADPH, has been crystallized by the hanging-drop method in a form apparently depleted in dinucleotide. The crystals belong to the hexagonal space group P6(2)22 with a = b = 111.7 A, c = 248.8 A. There is one subunit in the asymmetric unit. Data were collected to 2.9 A at the L.U.R.E. (Orsay) synchrotron radiation facility. The tetramers have been located in the crystal, centered on the site (1/2, 0, 0) with 222 symmetry.

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Year:  1991        PMID: 1942042     DOI: 10.1016/0022-2836(91)90918-v

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


  2 in total

1.  Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site.

Authors:  A Buzy; V Bracchi; R Sterjiades; J Chroboczek; P Thibault; J Gagnon; H M Jouve; G Hudry-Clergeon
Journal:  J Protein Chem       Date:  1995-02

2.  NADPH binding and control of catalase compound II formation: comparison of bovine, yeast, and Escherichia coli enzymes.

Authors:  A Hillar; P Nicholls; J Switala; P C Loewen
Journal:  Biochem J       Date:  1994-06-01       Impact factor: 3.857

  2 in total

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