Extracellular Loop 4 of the Proline Transporter PutP Controls the Periplasmic Entrance to Ligand Binding Sites

DC FieldValueLanguage
dc.contributor.authorRaba, Michael
dc.contributor.authorDunkel, Sabrina
dc.contributor.authorHilger, Daniel
dc.contributor.authorLipiszko, Kamila
dc.contributor.authorPolyhach, Yevhen
dc.contributor.authorJeschke, Gunnar
dc.contributor.authorBracher, Susanne
dc.contributor.authorKlare, Johann P.
dc.contributor.authorQuick, Matthias
dc.contributor.authorJung, Heinrich
dc.contributor.authorSteinhoff, Heinz-Juergen
dc.date.accessioned2021-12-23T16:21:37Z-
dc.date.available2021-12-23T16:21:37Z-
dc.date.issued2014
dc.identifier.issn09692126
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/13947-
dc.description.abstractThe Na+/proline symporter (PutP), like several other Na+-coupled symporters, belongs to the so-called LeuT-fold structural family, which features ten core transmembrane domains (cTMs) connected by extra- and intracellular loops. The role of these loops has been discussed in context with the gating function in the alternating access model of secondary active transport processes. Here we report the complete spin-labeling site scan of extracellular loop 4 (eL4) in PutP that reveals the presence of two alpha-helical segments, eL4a and eL4b. Among the eL4 residues that are directly implicated in the functional dynamics of the transporter, Phe314 in eL4b anchors the loop by means of hydrophobic contacts to cTM1 close to the ligand binding sites. We propose that ligand-induced conformational changes at the binding sites are transmitted via the anchoring residue to eL4 and through eL4 further to adjacent cTMs, leading to closure of the extracellular gate.
dc.description.sponsorshipElite Network of Bavaria; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [JU333/3-3, JU333/4-3, STE640/11]; SNF [20PA21E_ 129360/1]; We thank Sophie Dittmer for generation of mutants and functional analyses. We thank M. Cichon (group H.-J.S.) for EPR measurements. M.R. was supported by a fellowship of the Elite Network of Bavaria. This work was financially supported by the Deutsche Forschungsgemeinschaft grants JU333/3-3 and JU333/4-3 to H.J. and STE640/11 to H.-J.S. as well as SNF grant 20PA21E_ 129360/1 to G.J.
dc.language.isoen
dc.publisherCELL PRESS
dc.relation.ispartofSTRUCTURE
dc.subjectBACTERIAL HOMOLOG
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectCell Biology
dc.subjectCONFORMATIONAL-CHANGES
dc.subjectCRYSTAL-STRUCTURE
dc.subjectDISTANCE MEASUREMENTS
dc.subjectESCHERICHIA-COLI
dc.subjectMEMBRANE-TRANSPORT
dc.subjectMOLECULAR-BASIS
dc.subjectNA+/PROLINE TRANSPORTER
dc.subjectPROTEIN-STRUCTURE
dc.subjectTRANSMEMBRANE DOMAIN-IX
dc.titleExtracellular Loop 4 of the Proline Transporter PutP Controls the Periplasmic Entrance to Ligand Binding Sites
dc.typejournal article
dc.identifier.doi10.1016/j.str.2014.03.011
dc.identifier.isiISI:000335443700014
dc.description.volume22
dc.description.issue5
dc.description.startpage769
dc.description.endpage780
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0002-5761-5968
dc.contributor.orcid0000-0002-5450-3063
dc.contributor.orcid0000-0001-5179-1357
dc.contributor.researcheridH-3791-2014
dc.contributor.researcheridC-1428-2009
dc.contributor.researcheridK-3790-2014
dc.contributor.researcheridC-7297-2019
dc.identifier.eissn18784186
dc.publisher.place50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
dcterms.isPartOf.abbreviationStructure
dcterms.oaStatusBronze
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptidfb04-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidStHe633-
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