DC Field | Value | Language |
dc.contributor.author | Pulagam, Lakshmi Padmavathi | |
dc.contributor.author | Steinhoff, Heinz-Juergen | |
dc.date.accessioned | 2021-12-23T15:56:21Z | - |
dc.date.available | 2021-12-23T15:56:21Z | - |
dc.date.issued | 2013 | |
dc.identifier.issn | 00222836 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/2305 | - |
dc.description.abstract | Colicin A is a pore-forming toxin that forms a voltage-gated channel in the inner membrane of the target bacteria. The structures of the closed and open channel states of membrane-bound colicin A are not resolved. In the present site-directed spin-labeling study, the insertion-competent state of colicin A is provoked by an acidic pH jump prior to the insertion into liposomes prepared from Escherichia coli natural lipids. The membrane-bound colicin A is able to open a voltage-dependent channel as demonstrated by the efflux of tempophosphate spin label from the lumen of liposomes. The EPR spectra of spin-labeled colicin A variants in the membrane-bound closed channel state reveal a conformational equilibrium with resolved interhelical tertiary contacts. The spin label accessibility and polarity profiles suggest the amphipathic helices (H1-H7 and H10) to be located in the membrane close to the membrane-water interface and the hydrophobic hairpin (H8 and H9) to be immersed more deeply in the membrane. (C) 2013 Elsevier Ltd. All rights reserved. | |
dc.language.iso | en | |
dc.publisher | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | |
dc.relation.ispartof | JOURNAL OF MOLECULAR BIOLOGY | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | BOUND STATE | |
dc.subject | channel activity in liposomes | |
dc.subject | closed channel state | |
dc.subject | E1 CHANNEL DOMAIN | |
dc.subject | HELIX-G | |
dc.subject | HIGH-FIELD EPR | |
dc.subject | insertion-competent state | |
dc.subject | NITROXIDE MOTION | |
dc.subject | PORE-FORMING DOMAIN | |
dc.subject | PROTEIN | |
dc.subject | SIDE-CHAINS | |
dc.subject | site-directed spin labeling | |
dc.subject | STRUCTURAL DETERMINANTS | |
dc.subject | TRANSFER DISTANCE MEASUREMENTS | |
dc.subject | water-soluble pore-forming toxin | |
dc.title | Acidic pH-Induced Membrane Insertion of Colicin A into E. coli Natural Lipids Probed by Site-Directed Spin Labeling | |
dc.type | journal article | |
dc.identifier.doi | 10.1016/j.jmb.2013.01.037 | |
dc.identifier.isi | ISI:000319490100015 | |
dc.description.volume | 425 | |
dc.description.issue | 10 | |
dc.description.startpage | 1782 | |
dc.description.endpage | 1794 | |
dc.contributor.orcid | 0000-0002-5888-0157 | |
dc.contributor.researcherid | H-3791-2014 | |
dc.identifier.eissn | 10898638 | |
dc.publisher.place | 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND | |
dcterms.isPartOf.abbreviation | J. Mol. Biol. | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | StHe633 | - |