1H, 13C and 15N resonance assignment of the oxidized form (Cys67–Cys70) of the N-terminal domain of PilB from Neisseria meningitidis

Quinternet, Marc; Beaufils, Chrystel; Neiers, Fabrice; Tsan, Pascale; Boschi‐Muller, Sandrine; Averlant‐Petit, Marie‐Christine; Branlant, Guy; Cung, Manh Thông

doi:10.1007/s12104-007-9038-8

Cited by 2 publications

(3 citation statements)

References 9 publications

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“…That concerns residues Phe62, Ala64, Ser65, Cys67 to Ser72, Phe99 to His101, Pro140, and Ser141. These chemical shift data are consistent with the previously reported data concerning backbone amide groups and with local structural changes in the neighborhood of the active site occurring upon oxidation. Other but isolated residues are also perturbed (Leu37, Ala43, Leu52, and Gly118).…”

Section: Resultssupporting

confidence: 92%

“…NterPilB has been studied in a soluble form ranging from Val33 to Leu175. The chemical shift assignments for the reduced and oxidized forms have been reported previously , . For these two forms, a nearly complete assignment of the backbone and of the side chains has been realized except for the sequence Val33 to His35, residues Ser137 and Pro171.…”

Section: Resultsmentioning

confidence: 60%

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Solution Structure and Dynamics of the Reduced and Oxidized Forms of the N-Terminal Domain of PilB from Neisseria meningitidis

et al. 2008

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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.

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 60%

Solution Structure and Dynamics of the Reduced and Oxidized Forms of the N-Terminal Domain of PilB from Neisseria meningitidis

et al. 2008

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“…Compared with the free form assignment of both partners (Beaufils et al, 2006;Quinternet et al, 2007Quinternet et al, , 2008c, significant amide chemical shift changes upon complex formation (i.e., changes exhibiting more than one standard deviation of the Dd value) are observed in the E69-V76, G102-S103, and V108-V113 segments of nDsbD cx and for the S65, C67, S72, E73, H101, V138, S141 residues and the K156-S158 segment of NterPilB cx , as displayed in Figures 1D and 1F. Figures 1E and 1G show that these residues are located near the active sites.…”

Section: Assignment Of the Ndsbd-ss-nterpilb Complex And Chemical Shift Mappingmentioning

confidence: 99%

Formation of the Complex between DsbD and PilB N-Terminal Domains from Neisseria meningitidis Necessitates an Adaptability of nDsbD

et al. 2009

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DsbD transmembrane protein dispatches electrons to periplasmic Trx/DsbE-like partners via specific interactions with its N-terminal domain, nDsbD. In the present study, PilB N-terminal domain (NterPilB) is shown to efficiently accept electrons coming from nDsbD from Neisseria meningitidis. Using an NMR-driven docking approach, we have modeled the structure of a mixed disulfide complex between NterPilB and nDsbD. We show the needed opening of nDsbD cap-loop whereas NterPilB FLHE loop does not seem essential in the formation and stabilization of the complex. Relaxation analysis performed on backbone amide groups highlights a kind of dynamics transfer from nDsbD cap-loop on NterPilB alpha1 helix, suggesting that a mobility contribution is required not only for the formation of the mixed disulfide complex, but also for its disruption. Taking into account previous X-ray data on covalent complexes involving nDsbD, a cartoon of interactions between Trx-like partners and nDsbD is proposed that illustrates the adaptability of nDsbD.

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1H, 13C and 15N resonance assignment of the oxidized form (Cys67–Cys70) of the N-terminal domain of PilB from Neisseria meningitidis

Cited by 2 publications

References 9 publications

Solution Structure and Dynamics of the Reduced and Oxidized Forms of the N-Terminal Domain of PilB from Neisseria meningitidis

Solution Structure and Dynamics of the Reduced and Oxidized Forms of the N-Terminal Domain of PilB from Neisseria meningitidis

Formation of the Complex between DsbD and PilB N-Terminal Domains from Neisseria meningitidis Necessitates an Adaptability of nDsbD

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