Literature DB >> 25849513

Expression, purification, crystallization and preliminary X-ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogen Staphylococcus aureus.

Ana Lúcia Rosário1, Filipa V Sena1, Ana P Batista1, Tânia F Oliveira1, Diogo Athayde1, Manuela M Pereira1, José A Brito1, Margarida Archer1.   

Abstract

In recent years, type II NADH dehydrogenases (NDH-IIs) have emerged as potential drug targets for a wide range of human disease causative agents. In this work, the NDH-II enzyme from the Gram-positive human pathogen Staphylococcus aureus was recombinantly expressed in Escherichia coli, purified, crystallized and a crystallographic data set was collected at a wavelength of 0.873 Å. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 81.8, b = 86.0, c = 269.9 Å, contained four monomers per asymmetric unit and diffracted to a resolution of 3.32 Å. A molecular-replacement solution was obtained and model building and refinement are currently under way.

Entities:  

Keywords:  NADH dehydrogenase; NDH-II; Staphylococcus aureus; respiratory chain

Mesh:

Substances:

Year:  2015        PMID: 25849513      PMCID: PMC4388187          DOI: 10.1107/S2053230X15005178

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


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