2JZS

Solution structure of the reduced form of the N-terminal domain of PilB from N. meningitidis.

Summary for 2JZS

• Entry DOI: 10.2210/pdb2jzs/pdb
• Related: 2JZR
• Descriptor: Peptide methionine sulfoxide reductase msrA/msrB (1 entity in total)
• Functional Keywords: reduced, neisseria meningitidis, pilb, n-terminal domain, thioredoxin, electron transport, multifunctional enzyme, oxidoreductase, redox-active center, transport
• Biological source: Neisseria meningitidis serogroup A
• Total number of polymer chains: 1
• Total formula weight: 15848.09

Authors

Quinternet, M.,Tsan, P.,Neiers, F.,Beaufils, C.,Boschi-Muller, S.,Averlant-Petit, M.,Branlant, G.,Cung, M. (deposition date: 2008-01-15, release date: 2008-07-29, Last modification date: 2024-05-29)

Primary citation

Quinternet, M.,Tsan, P.,Neiers, F.,Beaufils, C.,Boschi-Muller, S.,Averlant-Petit, M.C.,Branlant, G.,Cung, M.T.
Solution structure and dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis.
Biochemistry, 47:8577-8589, 2008

PubMed Abstract: The secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive host's oxidative burst. PilB protein is composed of three domains. The central and the C-terminal domains display methionine sulfoxide reductase A and B activities, respectively. The N-terminal domain, which possesses a CXXC motif, was recently shown to regenerate in vitro the reduced forms of the methionine sulfoxide reductase domains of PilB from their oxidized forms, as does the thioredoxin 1 from E. coli, via a disulfide bond exchange. The thioredoxin-like N-terminal domain belongs to the cytochrome maturation protein structural family, but it possesses a unique additional segment (99)FLHE (102) localized in a loop. This segment covers one edge of the active site in the crystal structure of the reduced form of the N-terminal domain of PilB. We have determined the solution structure and the dynamics of the N-terminal domain from Neisseria meningitidis, in its reduced and oxidized forms. The FLHE loop adopts, in both redox states, a well-defined conformation. Subtle conformational and dynamic changes upon oxidation are highlighted around the active site, as well as in the FLHE loop. The functional consequences of the cytochrome maturation protein topology and those of the presence of FLHE loop are discussed in relation to the enzymatic properties of the N-terminal domain.

PubMed: 18651754
DOI: 10.1021/bi800884w

Experimental method

SOLUTION NMR