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000020004 084__ $$2WoS$$aBiochemistry & Molecular Biology
000020004 1001_ $$0P:(DE-HGF)0$$aCircolone, F.$$b0
000020004 245__ $$aStructural basis for the slow dark recovery of a full-length LOV protein from Pseudomonas putida
000020004 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2012
000020004 29510 $$a.
000020004 300__ $$a362 - 374
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000020004 440_0 $$03552$$aJournal of Molecular Biology$$v417$$x0022-2836$$y4
000020004 500__ $$aThe authors wish to thank Georg Buldt for continuous generous support and the scientists at beamline ID23-2 at the ESRF (Grenoble, France). Part of this work has been funded by the Deutsche Forschungsgemeinschaft within the GRK1166 "Biocatalysis in Non-Conventional Media".
000020004 520__ $$aBlue-light photoreceptors containing light–oxygen–voltage (LOV) domains regulate a myriad of different physiological responses in both eukaryotes and prokaryotes. Their light sensitivity is intricately linked to the photochemistry of the non-covalently bound flavin mononucleotide (FMN) chromophore that forms a covalent adduct with a conserved cysteine residue in the LOV domain upon illumination with blue light. All LOV domains undergo the same primary photochemistry leading to adduct formation; however, considerable variation is found in the lifetime of the adduct state that varies from seconds to several hours. The molecular mechanism underlying this variation among the structurally conserved LOV protein family is not well understood. Here, we describe the structural characterization of PpSB1-LOV, a very slow cycling full-length LOV protein from the Gram-negative bacterium Pseudomonas putida KT2440. Its crystal structure reveals a novel dimer interface that is mediated by N- and C-terminal auxiliary structural elements and a unique cluster of four arginine residues coordinating with the FMN-phosphate moiety. Site-directed mutagenesis of two arginines (R61 and R66) in PpSB1-LOV resulted in acceleration of the dark recovery reaction approximately by a factor of 280. The presented structural and biochemical data suggest a direct link between structural features and the slow dark recovery observed for PpSB1-LOV. The overall structural arrangement of PpSB1-LOV, together with a complementary phylogenetic analysis, highlights a common ancestry of bacterial LOV photoreceptors and Per-ARNT-Sim chemosensors.
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000020004 65320 $$2Author$$aphotoreceptor
000020004 65320 $$2Author$$aLOV domain
000020004 65320 $$2Author$$aPAS domain
000020004 65320 $$2Author$$acrystal structure
000020004 65320 $$2Author$$aphotocycle
000020004 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000020004 650_2 $$2MeSH$$aCrystallography, X-Ray
000020004 650_2 $$2MeSH$$aFlavin Mononucleotide: chemistry
000020004 650_2 $$2MeSH$$aLight
000020004 650_2 $$2MeSH$$aPhotoreceptors, Microbial: chemistry
000020004 650_2 $$2MeSH$$aProtein Structure, Tertiary
000020004 650_2 $$2MeSH$$aPseudomonas putida: metabolism
000020004 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000020004 650_7 $$00$$2NLM Chemicals$$aPhotoreceptors, Microbial
000020004 650_7 $$0146-17-8$$2NLM Chemicals$$aFlavin Mononucleotide
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000020004 7001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b1$$uFZJ
000020004 7001_ $$0P:(DE-HGF)0$$aJentzsch, K.$$b2
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000020004 7001_ $$0P:(DE-HGF)0$$aJaeger, K.E.$$b4
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000020004 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2012.01.056
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