Salt-driven equilibrium between two conformations in the HAMP domain from Natronomonas pharaonis - The language of signal transfer?

DC FieldValueLanguage
dc.contributor.authorDoebber, Meike
dc.contributor.authorBordignon, Enrica
dc.contributor.authorKlare, Johann P.
dc.contributor.authorHolterhues, Julia
dc.contributor.authorMartell, Swetlana
dc.contributor.authorMennes, Nadine
dc.contributor.authorLi, Lin
dc.contributor.authorEngelhard, Martin
dc.contributor.authorSteinhoff, Heinz-Juergen
dc.date.accessioned2021-12-23T16:10:08Z-
dc.date.available2021-12-23T16:10:08Z-
dc.date.issued2008
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/9171-
dc.description.abstractHAMP domains (conserved in histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins, and phosphatases) perform their putative function as signal transducing units in diversified environments in a variety of protein families. Here the conformational changes induced by environmental agents, namely salt and temperature, on the structure and function of a HAMP domain of the phototransducer from Natronomonas pharaonis (NpHtrII) in complex with sensory rhodopsin II (NpSRII) were investigated by site-directed spin labeling electron paramagnetic resonance. A series of spin labeled mutants were engineered in NpHtrII(157), a truncated analog containing only the first HAMP domain following the transmembrane helix 2. This truncated transducer is shown to be a valid model system for a signal transduction domain anchored to the transmembrane light sensor NpSRII. The HAMP domain is found to be engaged in a ``two-state'' equilibrium between a highly dynamic (dHAMP) and a more compact (cHAMP) conformation. The structural properties of the cHAMP as proven by mobility, accessibility, and intra-transducer-dimer distance data are in agreement with the four helical bundle NMR model of the HAMP domain from Archaeoglobus fulgidus.
dc.description.sponsorshipDeutsche Forschungsgemeinschaft GrantsGerman Research Foundation (DFG) [SFB 431/P18, EN87/14-2]; Max Planck SocietyMax Planck SocietyFoundation CELLEX; This work was supported by Deutsche Forschungsgemeinschaft Grants SFB 431/P18 (to J. P. K. and H. J. S.) and EN87/14-2 (to M. E.) and the Max Planck Society (to M. E.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked `` advertisement'' in accordance with 18 U. S. C. Section 1734 solely to indicate this fact.
dc.language.isoen
dc.publisherELSEVIER
dc.relation.ispartofJOURNAL OF BIOLOGICAL CHEMISTRY
dc.subjectBACTERIORHODOPSIN
dc.subjectBiochemistry & Molecular Biology
dc.subjectCOMPLEX
dc.subjectHISTIDINE KINASE
dc.subjectNITROXIDE MOTION
dc.subjectPHOBORHODOPSIN
dc.subjectPHOTOTRANSDUCER
dc.subjectSENSORY RHODOPSIN II
dc.subjectSIDE-CHAINS
dc.subjectSPIN-LABELED PROTEINS
dc.subjectSTRUCTURAL DETERMINANTS
dc.titleSalt-driven equilibrium between two conformations in the HAMP domain from Natronomonas pharaonis - The language of signal transfer?
dc.typejournal article
dc.identifier.doi10.1074/jbc.M801931200
dc.identifier.isiISI:000259969300071
dc.description.volume283
dc.description.issue42
dc.description.startpage28691
dc.description.endpage28701
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0002-5761-5968
dc.contributor.researcheridH-3791-2014
dc.contributor.researcheridC-1428-2009
dc.identifier.eissn1083351X
dc.publisher.placeRADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
dcterms.isPartOf.abbreviationJ. Biol. Chem.
dcterms.oaStatusGreen Published, hybrid
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptidfb04-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidStHe633-
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