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

页码：9 / 13

页数：5

共 44 条

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