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000085680 0247_ $$2doi$$a10.1002/prot.21700
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000085680 037__ $$aPHPPUBDB-8387
000085680 041__ $$aeng
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000085680 1001_ $$aMatrai, J.
000085680 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000085680 245__ $$aAn alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study
000085680 260__ $$aNew York, NY$$bWiley-Liss$$c2008
000085680 300__ $$a552-564
000085680 3367_ $$00$$2EndNote$$aJournal Article
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000085680 440_0 $$0PERI:(DE-600)1475032-6$$aProteins: Struct. Funct. Bioinf.$$v71$$x0887-3585$$y2
000085680 500__ $$3Converted on 2013-05-30 12:31
000085680 500__ $$3Converted on 2013-06-21 19:20
000085680 520__ $$aIn the present study, we report on the X-ray crystallographic structure of a GH32 invertase mutant, (i.e., the Arabidopsis thaliana cell-wall invertase 1-E203Q, AtcwINV1-mutant) in complex with sucrose. This structure was solved to reveal the features of sugar binding in the catalytic pocket. However, as demonstrated by the X-ray structure the sugar binding and the catalytic pocket arrangement is significantly altered as compared with what was expected based on previous X-ray structures on GH-J clan enzymes. We performed a series of docking and molecular dynamics simulations on various derivatives of AtcwINV1 to reveal the reasons behind this modified sugar binding. Our results demonstrate that the E203Q mutation introduced into the catalytic pocket triggers conformational changes that alter the wild type substrate binding. In addition, this study also reveals the putative productive sucrose binding modus in the wild type enzyme.
000085680 536__ $$0G:(DE-H253)POF1-No-Ref-20130405$$aFS Beamline without reference (POF1-550)$$cPOF1-550$$fPOF I$$x0
000085680 588__ $$aDataset connected to Pubmed
000085680 650_2 $$2MeSH$$aAmino Acid Substitution
000085680 650_2 $$2MeSH$$aArabidopsis: enzymology
000085680 650_2 $$2MeSH$$aComputer Simulation
000085680 650_2 $$2MeSH$$aCrystallization
000085680 650_2 $$2MeSH$$aCrystallography, X-Ray
000085680 650_2 $$2MeSH$$aModels, Molecular
000085680 650_2 $$2MeSH$$aProtein Conformation: drug effects
000085680 650_2 $$2MeSH$$aSucrose: metabolism
000085680 650_2 $$2MeSH$$abeta-Fructofuranosidase: chemistry
000085680 650_2 $$2MeSH$$abeta-Fructofuranosidase: genetics
000085680 650_2 $$2MeSH$$abeta-Fructofuranosidase: metabolism
000085680 650_7 $$057-50-1$$2NLM Chemicals$$aSucrose
000085680 650_7 $$0EC 3.2.1.26$$2NLM Chemicals$$abeta-Fructofuranosidase
000085680 693__ $$0EXP:(DE-H253)Unknown-BL-20150101$$6EXP:(DE-H253)Unknown-BL-20150101$$fUnknown DESY Beamline$$x0
000085680 7001_ $$aLammens, W.
000085680 7001_ $$aJonckheer, A.
000085680 7001_ $$aLe Roy, K.
000085680 7001_ $$aRabijns, A.
000085680 7001_ $$aVan den Ende, W.
000085680 7001_ $$aDe Maeyer, M.
000085680 773__ $$0PERI:(DE-600)1475032-6$$a10.1002/prot.21700$$gVol. 71, p. 552-564$$p552-564$$q71<552-564$$tProteins$$v71$$x0887-3585$$y2008
000085680 85640 $$uhttp://www3.interscience.wiley.com/cgi-bin/fulltext/116835267/PDFSTART
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000085680 9141_ $$a(c) 2008 Wiley-Liss, Inc., A Wiley Company$$y2008
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000085680 920_1 $$iEuropean Molecular Biology Laboratory$$kEMBL
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