000279385 001__ 279385
000279385 005__ 20210129221045.0
000279385 0247_ $$2doi$$a10.1371/journal.pone.0118548
000279385 0247_ $$2Handle$$a2128/9571
000279385 0247_ $$2WOS$$aWOS:000350314700037
000279385 0247_ $$2altmetric$$aaltmetric:3750989
000279385 0247_ $$2pmid$$apmid:25734798
000279385 037__ $$aFZJ-2015-07397
000279385 082__ $$a500
000279385 1001_ $$0P:(DE-Juel1)144613$$aBorshchevskiy, Valentin$$b0
000279385 245__ $$aStructural and functional investigation of flavin binding center of the NqrC subunit of sodium-translocating NADH:Quinone oxidoreductase from Vibrio harveyi
000279385 260__ $$aLawrence, Kan.$$bPLoS$$c2015
000279385 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1449756504_5828
000279385 3367_ $$2DataCite$$aOutput Types/Journal article
000279385 3367_ $$00$$2EndNote$$aJournal Article
000279385 3367_ $$2BibTeX$$aARTICLE
000279385 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000279385 3367_ $$2DRIVER$$aarticle
000279385 520__ $$aNa+-translocating NADH:quinone oxidoreductase (NQR) is a redox-driven sodium pump operating in the respiratory chain of various bacteria, including pathogenic species. The enzyme has a unique set of redox active prosthetic groups, which includes two covalently bound flavin mononucleotide (FMN) residues attached to threonine residues in subunits NqrB and NqrC. The reason of FMN covalent bonding in the subunits has not been established yet. In the current work, binding of free FMN to the apo-form of NqrC from Vibrio harveyi was studied showing very low affinity of NqrC to FMN in the absence of its covalent bonding. To study structural aspects of flavin binding in NqrC, its holo-form was crystallized and its 3D structure was solved at 1.56 Å resolution. It was found that the isoalloxazine moiety of the FMN residue is buried in a hydrophobic cavity and that its pyrimidine ring is squeezed between hydrophobic amino acid residues while its benzene ring is extended from the protein surroundings. This structure of the flavin-binding pocket appears to provide flexibility of the benzene ring, which can help the FMN residue to take the bended conformation and thus to stabilize the one-electron reduced form of the prosthetic group. These properties may also lead to relatively weak noncovalent binding of the flavin. This fact along with periplasmic location of the FMN-binding domains in the vast majority of NqrC-like proteins may explain the necessity of the covalent bonding of this prosthetic group to prevent its loss to the external medium.
000279385 536__ $$0G:(DE-HGF)POF3-551$$a551 - Functional Macromolecules and Complexes (POF3-551)$$cPOF3-551$$fPOF III$$x0
000279385 588__ $$aDataset connected to CrossRef
000279385 7001_ $$0P:(DE-HGF)0$$aRound, Ekaterina$$b1
000279385 7001_ $$0P:(DE-HGF)0$$aBertsova, Yulia$$b2
000279385 7001_ $$0P:(DE-HGF)0$$aPolovinkin, Vitaly$$b3
000279385 7001_ $$0P:(DE-Juel1)165798$$aGushchin, Ivan$$b4$$ufzj
000279385 7001_ $$0P:(DE-Juel1)131968$$aIshchenko, Andrii$$b5
000279385 7001_ $$0P:(DE-Juel1)165629$$aKovalev, Kirill$$b6
000279385 7001_ $$0P:(DE-HGF)0$$aMishin, Alexey$$b7
000279385 7001_ $$0P:(DE-HGF)0$$aKachalova, Galina$$b8
000279385 7001_ $$0P:(DE-HGF)0$$aPopov, Alexander$$b9
000279385 7001_ $$0P:(DE-HGF)0$$aBogachev, Alexander$$b10
000279385 7001_ $$0P:(DE-Juel1)131964$$aGordeliy, Valentin$$b11$$eCorresponding author$$ufzj
000279385 773__ $$0PERI:(DE-600)2267670-3$$a10.1371/journal.pone.0118548$$gVol. 10, no. 3, p. e0118548 -$$n3$$pe0118548$$tPLoS one$$v10$$x1932-6203$$y2015
000279385 8564_ $$uhttps://juser.fz-juelich.de/record/279385/files/Structural%20and%20functional%20investigation%20of%20flavin%20binding%20center%20of%20the%20NqrC%20subunit%20of%20sodium-translocating%20NADH%3Aquinone%20oxidoreductase%20from%20Vibrio%20harveyi.pdf$$yOpenAccess
000279385 8564_ $$uhttps://juser.fz-juelich.de/record/279385/files/Structural%20and%20functional%20investigation%20of%20flavin%20binding%20center%20of%20the%20NqrC%20subunit%20of%20sodium-translocating%20NADH%3Aquinone%20oxidoreductase%20from%20Vibrio%20harveyi.gif?subformat=icon$$xicon$$yOpenAccess
000279385 8564_ $$uhttps://juser.fz-juelich.de/record/279385/files/Structural%20and%20functional%20investigation%20of%20flavin%20binding%20center%20of%20the%20NqrC%20subunit%20of%20sodium-translocating%20NADH%3Aquinone%20oxidoreductase%20from%20Vibrio%20harveyi.jpg?subformat=icon-1440$$xicon-1440$$yOpenAccess
000279385 8564_ $$uhttps://juser.fz-juelich.de/record/279385/files/Structural%20and%20functional%20investigation%20of%20flavin%20binding%20center%20of%20the%20NqrC%20subunit%20of%20sodium-translocating%20NADH%3Aquinone%20oxidoreductase%20from%20Vibrio%20harveyi.jpg?subformat=icon-180$$xicon-180$$yOpenAccess
000279385 8564_ $$uhttps://juser.fz-juelich.de/record/279385/files/Structural%20and%20functional%20investigation%20of%20flavin%20binding%20center%20of%20the%20NqrC%20subunit%20of%20sodium-translocating%20NADH%3Aquinone%20oxidoreductase%20from%20Vibrio%20harveyi.jpg?subformat=icon-640$$xicon-640$$yOpenAccess
000279385 8564_ $$uhttps://juser.fz-juelich.de/record/279385/files/Structural%20and%20functional%20investigation%20of%20flavin%20binding%20center%20of%20the%20NqrC%20subunit%20of%20sodium-translocating%20NADH%3Aquinone%20oxidoreductase%20from%20Vibrio%20harveyi.pdf?subformat=pdfa$$xpdfa$$yOpenAccess
000279385 909CO $$ooai:juser.fz-juelich.de:279385$$pdnbdelivery$$pVDB$$pdriver$$popen_access$$popenaire
000279385 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)165798$$aForschungszentrum Jülich GmbH$$b4$$kFZJ
000279385 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131964$$aForschungszentrum Jülich GmbH$$b11$$kFZJ
000279385 9131_ $$0G:(DE-HGF)POF3-551$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vFunctional Macromolecules and Complexes$$x0
000279385 9141_ $$y2015
000279385 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000279385 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000279385 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
000279385 915__ $$0StatID:(DE-HGF)1040$$2StatID$$aDBCoverage$$bZoological Record
000279385 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bPLOS ONE : 2014
000279385 915__ $$0StatID:(DE-HGF)0500$$2StatID$$aDBCoverage$$bDOAJ
000279385 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000279385 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000279385 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000279385 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000279385 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000279385 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000279385 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000279385 920__ $$lyes
000279385 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000279385 9801_ $$aUNRESTRICTED
000279385 9801_ $$aFullTexts
000279385 980__ $$ajournal
000279385 980__ $$aVDB
000279385 980__ $$aUNRESTRICTED
000279385 980__ $$aI:(DE-Juel1)ICS-6-20110106
000279385 981__ $$aI:(DE-Juel1)IBI-7-20200312