Membrane Region M-2C2 in Subunit KtrB of the K+ Uptake System KtrAB from Vibrio alginolyticus Forms a Flexible Gate Controlling K+ Flux AN ELECTRON PARAMAGNETIC RESONANCE STUDY
DC Element | Wert | Sprache |
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dc.contributor.author | Haenelt, Inga | |
dc.contributor.author | Wunnicke, Dorith | |
dc.contributor.author | Mueller-Trimbusch, Meike | |
dc.contributor.author | Vor der Brueggen, Marc | |
dc.contributor.author | Kraus, Inga | |
dc.contributor.author | Bakker, Evert P. | |
dc.contributor.author | Steinhoff, Heinz-Juergen | |
dc.date.accessioned | 2021-12-23T16:11:57Z | - |
dc.date.available | 2021-12-23T16:11:57Z | - |
dc.date.issued | 2010 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/9970 | - |
dc.description.abstract | Transmembrane stretch M-2C from the bacterial K+-translocating protein KtrB is unusually long. In its middle part, termed M-2C2, it contains several small and polar amino acids. This region is flanked by the two alpha-helices M-2C1 and M-2C3 and may form a flexible gate at the cytoplasmic side of the membrane controlling K+ translocation. In this study, we provide experimental evidence for this notion by using continuous wave and pulse EPR measurements of single and double spin-labeled cysteine variants of KtrB. Most of the spin-labeled residues in M-2C2 were shown to be immobile, pointing to a compact structure. However, the high polarity revealed for the microenvironment of residue positions 317, 318, and 327 indicated the existence of a water-accessible cavity. Upon the addition of K+ ions, M2C2 residue Thr-318R1 (R1 indicates the bound spin label) moved with respect to M-2B residue Asp-222R1 and M2C3 residue Val-331R1 but not with respect to M2C1 residue Met-311R1. Based on distances determined between spin-labeled residues of double-labeled variants of KtrB in the presence and absence of K+ ions, structural models of the open and closed conformations were developed. | |
dc.description.sponsorship | Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB431]; This work was supported by the Deutsche Forschungsgemeinschaft SFB431 (projects P6 and P18). | |
dc.language.iso | en | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | |
dc.subject | AMINO-ACID SUBSTITUTIONS | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CRYSTAL-STRUCTURE | |
dc.subject | DISTANCE MEASUREMENTS | |
dc.subject | ESCHERICHIA-COLI K-12 | |
dc.subject | FULL-LENGTH KCSA | |
dc.subject | GLYCINE RESIDUES | |
dc.subject | HIGH-AFFINITY | |
dc.subject | ION CHANNEL | |
dc.subject | KDPFABC COMPLEX | |
dc.subject | POTASSIUM-TRANSPORT | |
dc.title | Membrane Region M-2C2 in Subunit KtrB of the K+ Uptake System KtrAB from Vibrio alginolyticus Forms a Flexible Gate Controlling K+ Flux AN ELECTRON PARAMAGNETIC RESONANCE STUDY | |
dc.type | journal article | |
dc.identifier.doi | 10.1074/jbc.M110.139311 | |
dc.identifier.isi | ISI:000281404100064 | |
dc.description.volume | 285 | |
dc.description.issue | 36 | |
dc.description.startpage | 28210 | |
dc.description.endpage | 28219 | |
dc.contributor.orcid | 0000-0003-1495-3163 | |
dc.contributor.orcid | 0000-0002-5888-0157 | |
dc.contributor.researcherid | N-2982-2016 | |
dc.contributor.researcherid | H-3791-2014 | |
dc.identifier.eissn | 1083351X | |
dc.publisher.place | 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA | |
dcterms.isPartOf.abbreviation | J. Biol. Chem. | |
dcterms.oaStatus | Green Published, hybrid | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | StHe633 | - |
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geprüft am 06.06.2024