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000090170 0247_ $$2pmid$$apmid:20006620
000090170 0247_ $$2doi$$a10.1016/j.jmb.2009.12.009
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000090170 0247_ $$2ISSN$$a0022-2836
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000090170 1001_ $$aKachalova, G. S.
000090170 1101_ $$aDESY$$bExperiments with synchrotron radiation$$bMax-Planck-Arbeitsgruppen
000090170 245__ $$aCrystal structure analysis of free and substrate-bound 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans
000090170 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2010
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000090170 440_0 $$0PERI:(DE-600)1355192-9$$aJ. Mol. Biol.$$v396$$x0022-2836
000090170 500__ $$3Converted on 2013-05-30 13:52
000090170 500__ $$3Converted on 2013-06-21 19:20
000090170 520__ $$aThe pathway for oxidative degradation of nicotine in Arthrobacter nicotinovorans includes two genetically and structurally unrelated flavoenzymes, 6-hydroxy-L-nicotine oxidase (6HLNO) and 6-hydroxy-D-nicotine oxidase, which act with absolute stereospecificity on the L- and D-forms, respectively, of 6-hydroxy-nicotine. We solved the crystal structure of 6HLNO at 1.95 A resolution by combined isomorphous/multiple-wavelength anomalous dispersion phasing. The overall structure of each subunit of the 6HLNO homodimer and the folds of the individual domains are closely similar as in eukaryotic monoamine oxidases. Unexpectedly, a diacylglycerophospholipid molecule was found to be non-covalently bound to each protomer of 6HLNO. The fatty acid chains occupy hydrophobic channels that penetrate deep into the interior of the substrate-binding domain of each subunit. The solvent-exposed glycerophosphate moiety is located at the subunit-subunit interface. We further solved the crystal structure of a complex of dithionite-reduced 6HLNO with the natural substrate 6-hydroxy-L-nicotine at 2.05 A resolution. The location of the substrate in a tight cavity suggests that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions. The observed orientation of the bound substrate relative to the isoalloxazine ring of the flavin adenine dinucleotide cofactor is suitable for hydride-transfer dehydrogenation at the carbon atom that forms the chiral center of the substrate molecule. A comparison of the substrate-binding modes of 6HLNO and 6-hydroxy-D-nicotine oxidase, based on models of complexes with the D-substrate, suggests an explanation for the stereospecificity of both enzymes. The two enzymes are proposed to orient the enantiomeric substrates in mirror symmetry with respect to the plane of the flavin.
000090170 536__ $$0G:(DE-H253)POF2-DORIS-PETRA-20130405$$aFacility (machine) DORIS/PETRA (POF2-DORIS-PETRA-20130405)$$cPOF2-DORIS-PETRA-20130405$$fPOF II$$x0
000090170 588__ $$aDataset connected to Pubmed
000090170 650_2 $$2MeSH$$aArthrobacter: enzymology
000090170 650_2 $$2MeSH$$aCrystallography, X-Ray
000090170 650_2 $$2MeSH$$aModels, Molecular
000090170 650_2 $$2MeSH$$aNicotine: analogs & derivatives
000090170 650_2 $$2MeSH$$aNicotine: metabolism
000090170 650_2 $$2MeSH$$aOxidoreductases Acting on CH-NH Group Donors: chemistry
000090170 650_2 $$2MeSH$$aPhosphatidic Acids: metabolism
000090170 650_2 $$2MeSH$$aProtein Binding
000090170 650_2 $$2MeSH$$aProtein Structure, Quaternary
000090170 650_2 $$2MeSH$$aProtein Subunits: chemistry
000090170 650_7 $$00$$2NLM Chemicals$$a6-hydroxynicotine
000090170 650_7 $$00$$2NLM Chemicals$$aPhosphatidic Acids
000090170 650_7 $$00$$2NLM Chemicals$$aProtein Subunits
000090170 650_7 $$054-11-5$$2NLM Chemicals$$aNicotine
000090170 650_7 $$0EC 1.5.-$$2NLM Chemicals$$aOxidoreductases Acting on CH-NH Group Donors
000090170 650_7 $$0EC 1.5.3.5$$2NLM Chemicals$$a6-hydroxy-L-nicotine oxidase
000090170 693__ $$0EXP:(DE-H253)DORISIII(machine)-20150101$$1EXP:(DE-H253)DORISIII-20150101$$5EXP:(DE-H253)DORISIII(machine)-20150101$$aDORIS III$$eFacility (machine) DORIS III$$x0
000090170 7001_ $$aBourenkov, G. P.
000090170 7001_ $$aMengesdorf, T.
000090170 7001_ $$aSchenk, S.
000090170 7001_ $$aMaun, H. R.
000090170 7001_ $$aBurghammer, M.
000090170 7001_ $$aRiekel, C.
000090170 7001_ $$aDecker, K.
000090170 7001_ $$aBartunik, H. D.
000090170 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2009.12.009$$gVol. 396, p. 785-799$$p785-799$$q396<785-799$$tJournal of molecular biology$$v396$$x0022-2836$$y2010
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000090170 9141_ $$a(c) Elsevier. No copyright permission for full text.$$y2010
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