000821076 001__ 821076
000821076 005__ 20210129224741.0
000821076 0247_ $$2doi$$a10.1016/j.jmb.2016.05.027
000821076 0247_ $$2ISSN$$a0022-2836
000821076 0247_ $$2ISSN$$a1089-8638
000821076 0247_ $$2WOS$$aWOS:000384383400005
000821076 0247_ $$2altmetric$$aaltmetric:8735861
000821076 0247_ $$2pmid$$apmid:27291287
000821076 037__ $$aFZJ-2016-06320
000821076 082__ $$a570
000821076 1001_ $$0P:(DE-Juel1)157880$$aRöllen, Katrin$$b0$$ufzj
000821076 245__ $$aSignaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy
000821076 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2016
000821076 3367_ $$2DRIVER$$aarticle
000821076 3367_ $$2DataCite$$aOutput Types/Journal article
000821076 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1484908763_27110
000821076 3367_ $$2BibTeX$$aARTICLE
000821076 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000821076 3367_ $$00$$2EndNote$$aJournal Article
000821076 520__ $$aLight–Oxygen–Voltage (LOV) domains represent the photo-responsive domains of various blue-light photoreceptor proteins and are widely distributed in plants, algae, fungi, and bacteria. Here, we report the dark-state crystal structure of PpSB1-LOV, a slow-reverting short LOV protein from Pseudomonas putida that is remarkably different from our previously published “fully light-adapted” structure [1]. A direct comparison of the two structures provides insight into the light-activated signaling mechanism. Major structural differences involve a ~11 Å movement of the C terminus in helix Jα, ~4 Å movement of Hβ–Iβ loop, disruption of hydrogen bonds in the dimer interface, and a ~29° rotation of chain-B relative to chain-A as compared to the light-state dimer. Both crystal structures and solution NMR data are suggestive of the key roles of a conserved glutamine Q116 and the N-cap region consisting of A′α–Aβ loop and the A′α helix in controlling the light-activated conformational changes. The activation mechanism proposed here for the PpSB1-LOV supports a rotary switch mechanism and provides insights into the signal propagation mechanism in naturally existing and artificial LOV-based, two-component systems and regulators.
000821076 536__ $$0G:(DE-HGF)POF3-553$$a553 - Physical Basis of Diseases (POF3-553)$$cPOF3-553$$fPOF III$$x0
000821076 536__ $$0G:(DE-HGF)POF3-581$$a581 - Biotechnology (POF3-581)$$cPOF3-581$$fPOF III$$x1
000821076 588__ $$aDataset connected to CrossRef
000821076 7001_ $$0P:(DE-Juel1)131965$$aGranzin, Joachim$$b1$$ufzj
000821076 7001_ $$0P:(DE-Juel1)157799$$aPanwalkar, Vineet$$b2$$ufzj
000821076 7001_ $$0P:(DE-Juel1)161543$$aArinkin, Vladimir$$b3$$ufzj
000821076 7001_ $$0P:(DE-Juel1)128547$$aRani, Raj$$b4
000821076 7001_ $$0P:(DE-Juel1)132001$$aHartmann, Rudolf$$b5$$ufzj
000821076 7001_ $$0P:(DE-Juel1)131482$$aKrauss, Ulrich$$b6$$ufzj
000821076 7001_ $$0P:(DE-Juel1)131457$$aJaeger, Karl-Erich$$b7$$ufzj
000821076 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b8$$ufzj
000821076 7001_ $$0P:(DE-Juel1)131950$$aBatra-Safferling, Renu$$b9$$eCorresponding author$$ufzj
000821076 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2016.05.027$$gVol. 428, no. 19, p. 3721 - 3736$$n19$$p3721 - 3736$$tJournal of molecular biology$$v428$$x0022-2836$$y2016
000821076 8564_ $$uhttps://juser.fz-juelich.de/record/821076/files/Signaling%20States%20of%20a%20Short%20Blue-Light%20Photoreceptor%20Protein%20PpSB1-LOV%20Revealed%20from%20Crystal%20Structures%20and%20Solution%20NMR%20Spectroscopy_2016.pdf$$yRestricted
000821076 8564_ $$uhttps://juser.fz-juelich.de/record/821076/files/Signaling%20States%20of%20a%20Short%20Blue-Light%20Photoreceptor%20Protein%20PpSB1-LOV%20Revealed%20from%20Crystal%20Structures%20and%20Solution%20NMR%20Spectroscopy_2016.gif?subformat=icon$$xicon$$yRestricted
000821076 8564_ $$uhttps://juser.fz-juelich.de/record/821076/files/Signaling%20States%20of%20a%20Short%20Blue-Light%20Photoreceptor%20Protein%20PpSB1-LOV%20Revealed%20from%20Crystal%20Structures%20and%20Solution%20NMR%20Spectroscopy_2016.jpg?subformat=icon-1440$$xicon-1440$$yRestricted
000821076 8564_ $$uhttps://juser.fz-juelich.de/record/821076/files/Signaling%20States%20of%20a%20Short%20Blue-Light%20Photoreceptor%20Protein%20PpSB1-LOV%20Revealed%20from%20Crystal%20Structures%20and%20Solution%20NMR%20Spectroscopy_2016.jpg?subformat=icon-180$$xicon-180$$yRestricted
000821076 8564_ $$uhttps://juser.fz-juelich.de/record/821076/files/Signaling%20States%20of%20a%20Short%20Blue-Light%20Photoreceptor%20Protein%20PpSB1-LOV%20Revealed%20from%20Crystal%20Structures%20and%20Solution%20NMR%20Spectroscopy_2016.jpg?subformat=icon-640$$xicon-640$$yRestricted
000821076 8564_ $$uhttps://juser.fz-juelich.de/record/821076/files/Signaling%20States%20of%20a%20Short%20Blue-Light%20Photoreceptor%20Protein%20PpSB1-LOV%20Revealed%20from%20Crystal%20Structures%20and%20Solution%20NMR%20Spectroscopy_2016.pdf?subformat=pdfa$$xpdfa$$yRestricted
000821076 909CO $$ooai:juser.fz-juelich.de:821076$$pVDB
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)157880$$aForschungszentrum Jülich$$b0$$kFZJ
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131965$$aForschungszentrum Jülich$$b1$$kFZJ
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)157799$$aForschungszentrum Jülich$$b2$$kFZJ
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)161543$$aForschungszentrum Jülich$$b3$$kFZJ
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132001$$aForschungszentrum Jülich$$b5$$kFZJ
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131482$$aForschungszentrum Jülich$$b6$$kFZJ
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131457$$aForschungszentrum Jülich$$b7$$kFZJ
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132029$$aForschungszentrum Jülich$$b8$$kFZJ
000821076 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131950$$aForschungszentrum Jülich$$b9$$kFZJ
000821076 9131_ $$0G:(DE-HGF)POF3-553$$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$$vPhysical Basis of Diseases$$x0
000821076 9131_ $$0G:(DE-HGF)POF3-581$$1G:(DE-HGF)POF3-580$$2G:(DE-HGF)POF3-500$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bKey Technologies$$lKey Technologies for the Bioeconomy$$vBiotechnology$$x1
000821076 9141_ $$y2016
000821076 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000821076 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000821076 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search
000821076 915__ $$0StatID:(DE-HGF)0550$$2StatID$$aNo Authors Fulltext
000821076 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bJ MOL BIOL : 2015
000821076 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000821076 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000821076 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000821076 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000821076 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC
000821076 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000821076 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000821076 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000821076 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000821076 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000821076 920__ $$lyes
000821076 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000821076 9201_ $$0I:(DE-Juel1)IMET-20090612$$kIMET$$lInstitut für Molekulare Enzymtechnologie (HHUD)$$x1
000821076 980__ $$ajournal
000821076 980__ $$aVDB
000821076 980__ $$aI:(DE-Juel1)ICS-6-20110106
000821076 980__ $$aI:(DE-Juel1)IMET-20090612
000821076 980__ $$aUNRESTRICTED
000821076 981__ $$aI:(DE-Juel1)IBI-7-20200312