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Preliminary crystallographic data of the three homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis.

Céline Lafaye 1, 2 Thomas Iwema 1, 3 Jean-Luc Ferrer 1, 3 J Simon Kroll 4 Mickael Griat 2 Laurence Serre 2, *
* Corresponding author
2 LPM - Laboratoire des Protéines Membranaires
IBS - UMR 5075 [1992-2019] - Institut de biologie structurale [1992-2019]
3 LCCP - Laboratoire de Cristallographie et Cristallogénèse des Protéines
IBS - UMR 5075 [1992-2019] - Institut de biologie structurale [1992-2019]
Abstract : Bacterial virulence depends on the correct folding of surface-exposed proteins, a process that is catalyzed by the thiol-disulfide oxidoreductase DsbA, which facilitates the synthesis of disulfide bonds in Gram-negative bacteria. Uniquely among bacteria, the Neisseria meningitidis genome possesses three genes encoding active DsbAs: DsbA1, DsbA2 and DsbA3. DsbA1 and DsbA2 have been characterized as lipoproteins involved in natural competence and in host-interactive biology, while the function of DsbA3 remains unknown. In an attempt to shed light on the reason for this multiplicity of dsbA genes, the three enzymes from N. meningitidis have been purified and crystallized in the presence of high concentrations of ammonium sulfate. The best crystals were obtained using DsbA1 and DsbA3; they belong to the orthorhombic and tetragonal systems and diffract to 1.5 and 2.7 A resolution, respectively.
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Céline Lafaye, Thomas Iwema, Jean-Luc Ferrer, J Simon Kroll, Mickael Griat, et al.. Preliminary crystallographic data of the three homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis.. Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd,, 2008, 64 (Pt 2), pp.111-4. ⟨10.1107/S1744309108000754⟩. ⟨inserm-00868614⟩

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