Substrate-Induced Conformational Changes in the S-Component ThiT from an Energy Coupling Factor Transporter

DC FieldValueLanguage
dc.contributor.authorMajsnerowska, Maria
dc.contributor.authorHanelt, Inga
dc.contributor.authorWunnicke, Dorith
dc.contributor.authorSchaefer, Lars V.
dc.contributor.authorSteinhoff, Heinz-Juergen
dc.contributor.authorSlotboom, Dirk Jan
dc.date.accessioned2021-12-23T16:16:05Z-
dc.date.available2021-12-23T16:16:05Z-
dc.date.issued2013
dc.identifier.issn09692126
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11714-
dc.description.abstractEnergy coupling factor (ECF) transporters are a recently discovered class of ABC transporters that mediate vitamin uptake in prokaryotes. Characteristic for ECF-type ABC transporters are small integral membrane proteins (S-components) that bind the transported substrates with high affinity. S-components associate with a second membrane protein (EcfT) and two peripheral ATPases to form a complete ATP-dependent transporter. Here, we have used EPR spectroscopy, stopped-flow fluorescence spectroscopy, and molecular dynamics simulations to determine the structural rearrangements that take place in the S-component ThiT from Lactococcus lactis upon binding of thiamin. Thiamin-induced conformational changes were confined to the long and partially membrane-embedded loop between transmembrane helices 1 and 2 that acts as a lid to occlude the binding site. The results indicate that solitary ThiT functions as a bona fide high-affinity substrate binding protein, which lacks a translocation pathway within the protein.
dc.description.sponsorshipNetherlands Organisation for Scientific research (NWO)Netherlands Organization for Scientific Research (NWO); EU (ERC)European Research Council (ERC)European Commission; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [STE 640/10]; EU (EDICT program); This work was supported by grants from The Netherlands Organisation for Scientific research (NWO: Vici and ALW Open Program grants to D.J.S.), the EU (ERC starting grant to D.J.S. and EDICT program), and the Deutsche Forschungsgemeinschaft (postdoctoral fellowship to I.H., grant STE 640/10 to H.J.S., and Emmy Noether grant to L.V.S.). We thank Arnau Cordomi for sharing the POPC force field parameters.
dc.language.isoen
dc.publisherCELL PRESS
dc.relation.ispartofSTRUCTURE
dc.subjectBILAYER
dc.subjectBINDING
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectCell Biology
dc.subjectEXPRESSION
dc.subjectFORCE-FIELDS
dc.subjectHOMOLOG
dc.subjectLINCS
dc.subjectLINEAR CONSTRAINT SOLVER
dc.subjectMECHANISM
dc.subjectMOLECULAR-DYNAMICS SIMULATIONS
dc.subjectPROTEINS
dc.titleSubstrate-Induced Conformational Changes in the S-Component ThiT from an Energy Coupling Factor Transporter
dc.typejournal article
dc.identifier.doi10.1016/j.str.2013.03.007
dc.identifier.isiISI:000318829400019
dc.description.volume21
dc.description.issue5
dc.description.startpage861
dc.description.endpage867
dc.contributor.orcid0000-0003-1495-3163
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0002-8498-3061
dc.contributor.researcheridN-2982-2016
dc.contributor.researcheridH-3791-2014
dc.contributor.researcheridW-7033-2019
dc.identifier.eissn18784186
dc.publisher.place50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
dcterms.isPartOf.abbreviationStructure
dcterms.oaStatusGreen Published, Bronze, Green Submitted
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptidfb04-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidStHe633-
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