2jzr | pdb_00002jzr

Solution structure of the oxidized form (Cys67-Cys70) of the N-terminal domain of PilB from N. meningitidis.

spinqualitylabelsall models 2jzr, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jzr is a 1 chain structure with sequence from Neisseria meningitidis serogroup a. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2jzs Gene: msrAB, pilB (Neisseria meningitidis serogroup A) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MSRAB_NEIMA] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Solution structure and dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis.,Quinternet M, Tsan P, Neiers F, Beaufils C, Boschi-Muller S, Averlant-Petit MC, Branlant G, Cung MT Biochemistry. 2008 Aug 19;47(33):8577-89. Epub 2008 Jul 24. PMID:18651754 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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