NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633

被引：4
|
作者：
Christ, Nina Alexandra [1 ,2 ]
Duchardt-Ferner, Elke [1 ,2 ]
Duesterhus, Stefanie [1 ]
Koetter, Peter [1 ]
Entian, Karl-Dieter [1 ]
Woehnert, Jens [1 ,2 ]
机构：
[1] Goethe Univ Frankfurt, Inst Mol Biowissensch, D-60438 Frankfurt, Germany
[2] Goethe Univ Frankfurt, Ctr Biomol Magnet Resonance BMRZ, D-60438 Frankfurt, Germany
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2012年 / 6卷 / 01期
关键词：
NMR-assignments; Triple resonance experiments; SpaI; Self-immunity; Lantibiotic; Subtilin; CHEMICAL-SHIFTS; LANTIBIOTICS; SPECTROSCOPY; BIOSYNTHESIS; EPIDERMIN; IMMUNITY; PORES; NISIN;
D O I：
10.1007/s12104-011-9314-5
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
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 H-1, N-15, C-13 chemical shift assignment for a stable 14.9 kDa C-terminal fragment of SpaI.
引用
收藏
页码：9 / 13
页数：5
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