PspA can form large scaffolds in Escherichia coli.

Standar, Kerstin; Mehner, Denise; Osadnik, Hendrik; Berthelmann, Felix; Hause, Gerd; Lünsdorf, Heinrich; Brüser, Thomas

dc.contributor.author	Standar, Kerstin
dc.contributor.author	Mehner, Denise
dc.contributor.author	Osadnik, Hendrik
dc.contributor.author	Berthelmann, Felix
dc.contributor.author	Hause, Gerd
dc.contributor.author	Lünsdorf, Heinrich
dc.contributor.author	Brüser, Thomas
dc.date.accessioned	2009-03-05T09:31:56Z
dc.date.available	2009-03-05T09:31:56Z
dc.date.issued	2008-10-29
dc.identifier.citation	PspA can form large scaffolds in Escherichia coli. 2008, 582 (25-26):3585-9 FEBS Lett.	en
dc.identifier.issn	0014-5793
dc.identifier.pmid	18789328
dc.identifier.doi	10.1016/j.febslet.2008.09.002
dc.identifier.uri	http://hdl.handle.net/10033/52253
dc.description.abstract	The phage shock protein A (PspA) of Escherichia coli stabilizes the cytoplasmic membrane under stress conditions. Here we demonstrate that PspA can form hollow spherical or prolate spheroidal particles of about 30-40nm diameter with a scaffold-like arrangement of protein subunits at the surface. The 'PspA-scaffold' is the basic structure that is common to all particles. The PspA-scaffold may be of fundamental importance, as it could allow PspA to stabilize the integrity of membranes through numerous contact points over a large surface area.
dc.language.iso	en	en
dc.subject.mesh	Bacterial Proteins	en
dc.subject.mesh	Cell Membrane	en
dc.subject.mesh	Escherichia coli	en
dc.subject.mesh	Escherichia coli Proteins	en
dc.subject.mesh	Heat-Shock Proteins	en
dc.title	PspA can form large scaffolds in Escherichia coli.	en
dc.type	Article	en
dc.contributor.department	Institute of Biology/Microbiology, University of Halle-Wittenberg, Kurt-Mothes-Strasse 3, D-06120 Halle, Germany.	en
dc.identifier.journal	FEBS letters	en
refterms.dateFOA	2018-06-13T03:57:30Z
html.description.abstract	The phage shock protein A (PspA) of Escherichia coli stabilizes the cytoplasmic membrane under stress conditions. Here we demonstrate that PspA can form hollow spherical or prolate spheroidal particles of about 30-40nm diameter with a scaffold-like arrangement of protein subunits at the surface. The 'PspA-scaffold' is the basic structure that is common to all particles. The PspA-scaffold may be of fundamental importance, as it could allow PspA to stabilize the integrity of membranes through numerous contact points over a large surface area.