Skip to Main content Skip to Navigation
Journal articles

Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis.

Abstract : Bacterial virulence depends on the correct folding of surface-exposed proteins, a process catalyzed by the thiol-disulfide oxidoreductase DsbA, which facilitates the synthesis of disulfide bonds in Gram-negative 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. This work reports the biochemical characterization of the three neisserial enzymes and the crystal structures of DsbA1 and DsbA3. As predicted by sequence homology, both enzymes adopt the classic Escherichia coli DsbA fold. The most striking feature shared by all three proteins is their exceptional oxidizing power. With a redox potential of -80 mV, the neisserial DsbAs are the most oxidizing thioredoxin-like enzymes known to date. Consistent with these findings, thermal studies indicate that their reduced form is also extremely stable. For each of these enzymes, this study shows that a threonine residue found within the active-site region plays a key role in dictating this extraordinary oxidizing power. This result highlights how residues located outside the CXXC motif may influence the redox potential of members of the thioredoxin family.
Document type :
Journal articles
Complete list of metadatas

Cited literature [49 references]  Display  Hide  Download

https://www.hal.inserm.fr/inserm-00869150
Contributor : Isabelle Arnal <>
Submitted on : Wednesday, October 2, 2013 - 2:58:45 PM
Last modification on : Thursday, November 19, 2020 - 8:50:29 AM
Long-term archiving on: : Friday, April 7, 2017 - 5:22:17 AM

File

 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document

Identifiers

Collections

Citation

Céline Lafaye, Thomas Iwema, Philippe Carpentier, Céline Juillan-Binard, J Simon Kroll, et al.. Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis.. Journal of Molecular Biology, Elsevier, 2009, 392 (4), pp.952-66. ⟨10.1016/j.jmb.2009.07.056⟩. ⟨inserm-00869150⟩

Share

Metrics

Record views

400