Transmembrane Signaling in the Maltose ABC Transporter MalFGK(2)-E PERIPLASMIC MalF-P2 LOOP COMMUNICATES SUBSTRATE AVAILABILITY TO THE ATP-BOUND MalK DIMER

DC FieldValueLanguage
dc.contributor.authorGrote, Mathias
dc.contributor.authorPolyhach, Yevhen
dc.contributor.authorJeschke, Gunnar
dc.contributor.authorSteinhoff, Heinz-Juergen
dc.contributor.authorSchneider, Erwin
dc.contributor.authorBordignon, Enrica
dc.date.accessioned2021-12-23T16:16:26Z-
dc.date.available2021-12-23T16:16:26Z-
dc.date.issued2009
dc.identifier.issn00219258
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11874-
dc.description.abstractABC transporters are ubiquitous membrane proteins that translocate solutes across biological membranes at the expense of ATP. In prokaryotic ABC importers, the extracytoplasmic anchoring of the substrate-binding protein (receptor) is emerging as a key determinant for the structural rearrangements in the cytoplasmically exposed ATP-binding cassette domains and in the transmembrane gates during the nucleotide cycle. Here the molecular mechanism of such signaling events was addressed by electron paramagnetic resonance spectroscopy of spin-labeled ATP-binding cassette maltose transporter variants (MalFGK(2)-E). A series of doubly spin-labeled mutants in the MalF-P2 domain involving positions 92, 205, 239, 252, and 273 and one triple mutant labeled at positions 205/252 in P2 and 83 in the Q-loop of MalK were assayed. The EPR data revealed that the substrate-binding protein MalE is bound to the transporter throughout the transport cycle. Concomitantly with the three conformations of the ATP-binding cassette MalK(2), three functionally relevant conformations are found also in the periplasmic MalF-P2 loop, strictly dependent on cytoplasmic nucleotide binding and periplasmic docking of liganded MalE to MalFG. The reciprocal communication across the membrane unveiled here gives first insights into the stimulatory effect of MalE on the ATPase activity, and it is suggested to be an important mechanistic feature of receptor-coupled ABC transporters.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SCHN 274/9-3, STE 640/7]; German National Academic Foundation; This work was supported by Deutsche Forschungsgemeinschaft Grants SCHN 274/9-3 (to E. S.) and STE 640/7 (to H.- J. S.) and by a fellowship from the German National Academic Foundation (to M. G.).
dc.language.isoen
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.relation.ispartofJOURNAL OF BIOLOGICAL CHEMISTRY
dc.subjectBINDING CASSETTE TRANSPORTER
dc.subjectBiochemistry & Molecular Biology
dc.subjectCATALYTIC CYCLE
dc.subjectCOMPLEX
dc.subjectELECTRON-PARAMAGNETIC-RESONANCE
dc.subjectESCHERICHIA-COLI
dc.subjectINTERACTS
dc.subjectP2
dc.subjectPROTEIN MALE
dc.subjectSALMONELLA
dc.subjectTYPHIMURIUM
dc.titleTransmembrane Signaling in the Maltose ABC Transporter MalFGK(2)-E PERIPLASMIC MalF-P2 LOOP COMMUNICATES SUBSTRATE AVAILABILITY TO THE ATP-BOUND MalK DIMER
dc.typejournal article
dc.identifier.doi10.1074/jbc.M109.006270
dc.identifier.isiISI:000267202500018
dc.description.volume284
dc.description.issue26
dc.description.startpage17521
dc.description.endpage17526
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.researcheridH-3791-2014
dc.identifier.eissn1083351X
dc.publisher.place9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
dcterms.isPartOf.abbreviationJ. Biol. Chem.
dcterms.oaStatusGreen Published, hybrid
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptidfb04-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidStHe633-
crisitem.author.netidScEr001-
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