2h30
Crystal structure of the N-terminal domain of PilB from Neisseria gonorrhoeae
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OverviewOverview
The PilB protein from Neisseria gonorrhoeae is located in the periplasm, and made up of three domains. The N-terminal, thioredoxin-like domain (NT, domain) is fused to tandem methionine sulfoxide reductase A and B domains, (MsrA/B). We show that the alpha domain of Escherichia coli DsbD is able, to reduce the oxidized NT domain, which suggests that DsbD in Neisseria, can transfer electrons from the cytoplasmic thioredoxin to the periplasm, for the reduction of the MsrA/B domains. An analysis of the available, complete genomes provides further evidence for this proposition in other, bacteria where DsbD/CcdA, Trx, MsrA, and MsrB gene homologs are all, located in a gene cluster with a common transcriptional direction. An, examination of wild-type PilB and a panel of Cys to Ser mutants of the, full-length protein and the individually expressed domains have also shown, that the NT domain more efficiently reduces the MsrA/B domains when in the, polyprotein context. Within this frame-work there does not appear to be a, preference for the NT domain to reduce the proximal MsrA domain over MsrB, domain. Finally, we report the 1.6A crystal structure of the NT domain., This structure confirms the presence of a surface loop that makes it, different from other membrane-tethered, Trx-like molecules, including, TlpA, CcmG, and ResA. Subtle differences are observed in this loop when, compared with the Neisseria meningitidis NT domain structure. The data, taken together supports the formation of specific NT domain interactions, with the MsrA/B domains and its in vivo recycling partner, DsbD.
About this StructureAbout this Structure
2H30 is a Single protein structure of sequence from Neisseria gonorrhoeae. Active as Peptide-methionine-(S)-S-oxide reductase, with EC number 1.8.4.11 Full crystallographic information is available from OCA.
ReferenceReference
The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases., Brot N, Collet JF, Johnson LC, Jonsson TJ, Weissbach H, Lowther WT, J Biol Chem. 2006 Oct 27;281(43):32668-75. Epub 2006 Aug 22. PMID:16926157
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