The X-ray structure of the N-terminal domain of PILB from Neisseria meningitidis reveals a thioredoxin-fold

Journal of Molecular Biology
Fanomezana M RanaivosonFrédérique Favier

Abstract

The secreted form of the PilB protein was recently shown to be bound to the outer membrane of Neisseria gonorrhoeae and proposed to be involved in survival of the pathogen to the host's oxidative burst. PilB is composed of three domains. The central and the C-terminal domains display methionine sulfoxide reductase (Msr) A and B activities respectively, i.e. the ability to reduce specifically the S and the R enantiomers of the sulfoxide function of the methionine sulfoxides, which are easily formed upon oxidation of methionine residues. The N-terminal domain of PilB (Dom1(PILB)) of N.meningitidis, which possesses a CXXC motif, was recently shown to recycle the oxidized forms of the PilB Msr domains in vitro, as the Escherichia coli thioredoxin (Trx) 1 does. The X-ray structure of Dom1(PILB) of N.meningitidis determined here shows a Trx-fold, in agreement with the biochemical properties of Dom1(PILB). However, substantial structural differences with E.coli Trx1 exist. Dom1(PILB) displays more structural homologies with the periplasmic disulfide oxidoreductases involved in cytochrome maturation pathways in bacteria. The active site of the reduced form of Dom1(PILB) reveals a high level of stabilization of the N-terminal catalytic ...Continue Reading

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Citations

Jun 5, 2012·The Journal of Biological Chemistry·Jung Chae LimRodney L Levine
May 11, 2015·FEBS Letters·Isabelle S ArtsJean-François Collet
Sep 8, 2009·Journal of Molecular Biology·Fanomezana M RanaivosonFrédérique Favier
Feb 8, 2008·Journal of Molecular Biology·Fanomezana M RanaivosonFrédérique Favier
Feb 28, 2008·Archives of Biochemistry and Biophysics·Sandrine Boschi-MullerGuy Branlant

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