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000016685 0247_ $$2DOI$$a10.1074/jbc.M110.206813
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000016685 084__ $$2WoS$$aBiochemistry & Molecular Biology
000016685 1001_ $$0P:(DE-Juel1)VDB101251$$aZerrad, L.$$b0$$uFZJ
000016685 245__ $$aA Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase.
000016685 260__ $$aBethesda, Md.$$bSoc.$$c2011
000016685 300__ $$a14040 - 14048
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000016685 440_0 $$03091$$aJournal of Biological Chemistry$$v286$$x0021-9258
000016685 500__ $$3POF3_Assignment on 2016-02-29
000016685 500__ $$aThis work was supported in part by Hungarian National Research Grant 77978.
000016685 520__ $$aPhosphoglycerate kinase (PGK) is the enzyme responsible for the first ATP-generating step of glycolysis and has been implicated extensively in oncogenesis and its development. Solution small angle x-ray scattering (SAXS) data, in combination with crystal structures of the enzyme in complex with substrate and product analogues, reveal a new conformation for the resting state of the enzyme and demonstrate the role of substrate binding in the preparation of the enzyme for domain closure. Comparison of the x-ray scattering curves of the enzyme in different states with crystal structures has allowed the complete reaction cycle to be resolved both structurally and temporally. The enzyme appears to spend most of its time in a fully open conformation with short periods of closure and catalysis, thereby allowing the rapid diffusion of substrates and products in and out of the binding sites. Analysis of the open apoenzyme structure, defined through deformable elastic network refinement against the SAXS data, suggests that interactions in a mostly buried hydrophobic region may favor the open conformation. This patch is exposed on domain closure, making the open conformation more thermodynamically stable. Ionic interactions act to maintain the closed conformation to allow catalysis. The short time PGK spends in the closed conformation and its strong tendency to rest in an open conformation imply a spring-loaded release mechanism to regulate domain movement, catalysis, and efficient product release.
000016685 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000016685 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000016685 588__ $$aDataset connected to Web of Science, Pubmed
000016685 650_2 $$2MeSH$$aAdenosine Triphosphate: chemistry
000016685 650_2 $$2MeSH$$aAmino Acid Sequence
000016685 650_2 $$2MeSH$$aAnimals
000016685 650_2 $$2MeSH$$aBinding Sites
000016685 650_2 $$2MeSH$$aBiophysics: methods
000016685 650_2 $$2MeSH$$aCatalysis
000016685 650_2 $$2MeSH$$aCrystallography, X-Ray: methods
000016685 650_2 $$2MeSH$$aHumans
000016685 650_2 $$2MeSH$$aMice
000016685 650_2 $$2MeSH$$aMolecular Sequence Data
000016685 650_2 $$2MeSH$$aPhosphoglycerate Kinase: chemistry
000016685 650_2 $$2MeSH$$aProtein Conformation
000016685 650_2 $$2MeSH$$aProtein Structure, Secondary
000016685 650_2 $$2MeSH$$aProtein Structure, Tertiary
000016685 650_2 $$2MeSH$$aScattering, Radiation
000016685 650_2 $$2MeSH$$aSequence Homology, Amino Acid
000016685 650_2 $$2MeSH$$aThermodynamics
000016685 650_7 $$056-65-5$$2NLM Chemicals$$aAdenosine Triphosphate
000016685 650_7 $$0EC 2.7.2.3$$2NLM Chemicals$$aPhosphoglycerate Kinase
000016685 650_7 $$2WoSType$$aJ
000016685 7001_ $$0P:(DE-Juel1)VDB101252$$aMerli, A.$$b1$$uFZJ
000016685 7001_ $$0P:(DE-Juel1)132018$$aSchröder, G.F.$$b2$$uFZJ
000016685 7001_ $$0P:(DE-Juel1)VDB101253$$aVarga, A.$$b3$$uFZJ
000016685 7001_ $$0P:(DE-Juel1)VDB101254$$aGráczer, E.$$b4$$uFZJ
000016685 7001_ $$0P:(DE-Juel1)VDB101255$$aPernot, P.$$b5$$uFZJ
000016685 7001_ $$0P:(DE-Juel1)VDB101256$$aRound, A.$$b6$$uFZJ
000016685 7001_ $$0P:(DE-Juel1)VDB101257$$aVas, M.$$b7$$uFZJ
000016685 7001_ $$0P:(DE-Juel1)VDB101258$$aBowler, M.W.$$b8$$uFZJ
000016685 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M110.206813$$gVol. 286, p. 14040 - 14048$$p14040 - 14048$$q286<14040 - 14048$$tThe @journal of biological chemistry$$v286$$x0021-9258$$y2011
000016685 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3077604
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000016685 9132_ $$0G:(DE-HGF)POF3-559H$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vAddenda$$x0
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