Bacillus subtilis ATCC 6633 produces the lipid II targeting lantibiotic subtilin. For self-protection these gram-positive bacteria express a cluster of four self-immunity proteins named SpaIFEG. SpaI is a 16.8*kDa lipoprotein which is attached to the outside of the cytoplasmic membrane via a covalently linked diacylglycerol anchor. Together with the ABC-transporter SpaFEG, SpaI protects the membrane from subtilin insertion and there is evidence for a direct interaction of SpaI with subtilin. As a prerequisite for further structural studies of SpaI and the SpaI/subtilin complex we report here the full (1)H, (15)N, (13)C chemical shift assignment for a stable 14.9 kDa C-terminal fragment of SpaI.
PMID: 21643970 [PubMed - as supplied by publisher]
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Biochemistry. 2010 Sep 15;
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Protein folding intermediates are often imperative to overall folding processes and consequent biological functions. However, the low population and transient nature of the intermediate states often hinder the biochemical and biophysical characterization. Previous studies have demonstrated that Bacillus...
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Eur J...
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Protein Sci. 1992 Oct;1(10):1363-76
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A low resolution...
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Biochemistry. 1990 Aug 7;29(31):7191-200
Authors: Wittekind M, Reizer J, Klevit RE
On the basis of an analysis of two-dimensional 1H NMR spectra, the complete sequence-specific 1H NMR assignments are presented for the phosphocarrier protein HPr from the...
NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633.
Linear Mode
