Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis
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- 作者：Ladislav Bumba (1)
Ekaterina Sviridova (2) (3)
Ivana Kutá Smatanová (2) (4)
Pavlína ?ezá?ová (5)
Václav Veverka (5) - 关键词：Neisseria meningitidis ; FrpC ; FrpD ; Backbone assignments ; NMR ; Iron ; regulated protein
- 刊名：Biomolecular NMR Assignments
- 出版年：2014
- 出版时间：April 2014
- 年：2014
- 卷：8
- 期：1
- 页码：53-55
- 全文大小：508 KB
- 参考文献：1. Bax A (1994) Multidimensional nuclear-magnetic-resonance methods for protein studies. Curr Opin Struct Biol 4(5):738-44 k" title="It opens in new window">CrossRef
2. Grifantini R, Sebastian S, Frigimelica E, Draghi M, Bartolini E, Muzzi A, Rappuoli R, Grandi G, Genco CA (2003) Identification of iron-activated and -repressed Fur-dependent genes by transcriptome analysis of / Neisseria meningitidis group B. Proc Natl Acad Sci USA 100(16):9542-547. doi:10.1073/pnas.1033001100 k" title="It opens in new window">CrossRef
3. Prochazkova K, Osicka R, Linhartova I, Halada P, Sulc M, Sebo P (2005) The / Neisseria meningitidis outer membrane lipoprotein FrpD binds the RTX protein FrpC. J Biol Chem 280(5):3251-258. doi:10.1074/jbc.M411232200 k" title="It opens in new window">CrossRef
4. Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS?+?: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213-23. doi:10.1007/s10858-009-9333-z k" title="It opens in new window">CrossRef
5. Sviridova E, Bumba L, Rezacova P, Prochazkova K, Kavan D, Bezouska K, Kuty M, Sebo P, Kuta Smatanova I (2010) Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD from / Neisseria meningitidis. Acta Crystallogr, Sect F: Struct Biol Cryst Commun 66(Pt 9):1119-123. doi:10.1107/S174430911003215X k" title="It opens in new window">CrossRef - 作者单位：Ladislav Bumba (1)
Ekaterina Sviridova (2) (3)
Ivana Kutá Smatanová (2) (4)
Pavlína ?ezá?ová (5)
Václav Veverka (5)
1. Institute of Microbiology of the ASCR, v.v.i., Videnska 1083, Prague, 142 20, Czech Republic
2. School of Complex Systems FFPW and CENAKVA, University of South Bohemia, Zamek 136, Nove Hrady, 373 33, Czech Republic
3. Faculty of Science, University of South Bohemia in ?eské Budějovice, Branisovska 31, 370 05, Ceske Budejovice, Czech Republic
4. Institute of Nanobiology and Structural Biology GCRC of the ASCR, v.v.i., Zamek 136, 373 33, Nove Hrady, Czech Republic
5. Institute of Organic Chemistry and Biochemistry of the ASCR, v.v.i., Flemingovo nam. 2, Prague, 166 10, Czech Republic - ISSN：1874-270X
文摘
The iron-regulated FrpD protein is a unique lipoprotein embedded into the outer membrane of the Gram-negative bacterium Neisseria meningitidis. The biological function of FrpD remains unknown but might consist in anchoring to the bacterial cell surface the Type I-secreted FrpC protein, which belongs to a Repeat in ToXins (RTX) protein family and binds FrpD with very high affinity (K d ?=?0.2 nM). Here, we report the backbone 1H, 13C, and 15N chemical shift assignments for the FrpD43-71 protein that allow us to characterize the intimate interaction between FrpD and the N-terminal domain of FrpC.