Preliminary crystallographic data of the three homologues of the thiol–disulfide oxidoreductase DsbA in Neisseria meningitidis. Corrigendum
نویسندگان
چکیده
Laboratoire des Protéines Membranaires, Institut de Biologie Structurale, CEA/CNRS/ Université Joseph Fourier, 41 Rue Jules Horowitz, 38027 Grenoble CEDEX 01, France, Laboratoire de Cristallogénèse et Cristallisation des Protéines, Institut de Biologie Structurale, CEA/CNRS/Université Joseph Fourier, 41 Rue Jules Horowitz, 38027 Grenoble CEDEX 01, France, and Department of Paediatrics, Imperial College London, St Mary’s Hospital Campus, Norfolk Place, London W2 1PG, England
منابع مشابه
Preliminary crystallographic data of the three homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis.
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...
متن کاملFunctional diversity of three different DsbA proteins from Neisseria meningitidis.
The genome of Neisseria meningitidis serogroup B strain MC58 contains three genes - nmb0278, nmb0294 and nmb0407 - encoding putative homologues of DsbA, a periplasmic thiol disulphide oxidoreductase protein-folding catalyst of the Dsb protein family. DsbA assists the folding of periplasmic and membrane proteins in diverse organisms. While all three cloned genes complemented the DTT sensitivity ...
متن کاملMutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.
Disulfide bond formation occurs in secreted proteins in Escherichia coli when the disulfide oxidoreductase DsbA, a soluble periplasmic protein, nonspecifically transfers a disulfide to a substrate protein. The catalytic disulfide of DsbA is regenerated by the inner-membrane protein DsbB. To help identify the specificity determinants in DsbB and to understand the nature of the kinetic barrier pr...
متن کاملRequirement of signal peptidase ComC and thiol-disulfide oxidoreductase DsbA for optimal cell surface display of pseudopilin ComGC in Staphylococcus aureus.
Staphylococcus aureus is an important Gram-positive bacterial pathogen producing many secreted and cell surface-localized virulence factors. Here we report that the staphylococcal thiol-disulfide oxidoreductase DsbA is essential for stable biogenesis of the ComGC pseudopilin. The signal peptidase ComC is indispensable for ComGC maturation and optimal cell surface exposure.
متن کاملRandomization of the Entire Active-site Helix 1 of the Thiol-disulfide Oxidoreductase DsbA from Escherichia coli*□S
DsbA from Escherichia coli is the most oxidizing member of the thiol-disulfide oxidoreductase family (Eo 122 mV) and is required for efficient disulfide bond formation in the periplasm. The reactivity of the catalytic disulfide bond (Cys-Pro-His-Cys) is primarily due to an extremely low pKa value (3.4) of Cys , which is stabilized by the partial positive dipole charge of the active-site helix 1...
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ورودعنوان ژورنال:
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications
دوره 64 شماره
صفحات -
تاریخ انتشار 2008