Structural and functional characterization of the Curli adaptor protein CsgF

被引：19

作者：

Schubeis, Tobias ^{[1
,2
]}

Spehr, Johannes ^{[1
,3
]}

Viereck, Janika ^{[1
,4
]}

Koepping, Laura ^{[1
,5
]}

Nagaraj, Madhu ^{[1
,6
]}

Ahmed, Mumdooh ^{[1
,7
]}

Ritter, Christiane ^{[1
]}

机构：

[1] Helmholtz Ctr Infect Res, Lab Macromol Interact, Braunschweig, Germany

[2] UCB Lyon 1, ENS Lyon, UMR CNRS 5280, Inst Sci Analyt, Villeurbanne, France

[3] Cellex Patient Treatment GmbH, Dresden, Germany

[4] Hannover Med Sch, Integriertes Forsch & Behandlungszentrum Transpla, IMTTS, D-30625 Hannover, Germany

[5] Univ Michigan, Dept Internal Med, Div Infect Dis, Ann Arbor, MI 48109 USA

[6] Aarhus Univ, Interdisciplinary Nanosci Ctr iNANO, Aarhus, Denmark

[7] Leibniz Univ Hannover, Ctr Biomol Drug Res, Hannover, Germany

来源：

FEBS LETTERS | 2018年 / 592卷 / 06期

关键词：

Curli; detergent micelles; functional amyloid; intrinsically disordered proteins; paramagnetic relaxation enhancement; solution NMR; NMR-SPECTROSCOPY; SECRETION; INSIGHTS; AGGREGATION; ORGANELLES; CHAPERONE;

D O I：

10.1002/1873-3468.13002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Curli are functional amyloids that form a major part of the biofilm produced by many enterobacteriaceae. A multiprotein system around the outer membrane protein CsgG is in charge of the export and controlled propagation of the main Curli subunits, CsgA and CsgB. CsgF is essential for the linkage of the main amyloid-forming proteins to the cell surface. Here, we present a profound biochemical and biophysical characterization of recombinant CsgF, highlighted by a solution NMR structure of CsgF in the presence of dihexanoylphosphocholine micelles. Interestingly, CsgF contains large unstructured domains and does not show a globular fold. The data presented shed new light on the molecular mechanism of Curli amyloid surface attachment.

引用

页码：1020 / 1029

页数：10

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