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000858361 1001_ $$0P:(DE-HGF)0$$aAtkinson, Sarah C.$$b0
000858361 245__ $$aSubstrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target
000858361 260__ $$aCambridge, Mass.$$bCell Press$$c2018
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000858361 520__ $$aProtein dynamics manifested through structural flex-ibility play a central role in the function of biologicalmolecules. Here we explore the substrate-mediatedchange in protein flexibility of an antibiotic targetenzyme, Clostridium botulinum dihydrodipicolinatesynthase. We demonstrate that the substrate, pyru-vate, stabilizes the more active dimer-of-dimers ortetrameric form. Surprisingly, there is little differencebetween the crystal structures of apo and substrate-bound enzyme, suggesting protein dynamics may beimportant. Neutron and small-angle X-ray scatteringexperiments were used to probe substrate-induceddynamics on the sub-second timescale, but nosignificant changes were observed. We thereforedeveloped a simple technique, coined protein dy-namics-mass spectrometry (ProD-MS), which en-ables measurement of time-dependent alkylation ofcysteine residues. ProD-MS together with X-raycrystallography and analytical ultracentrifugationanalyses indicates that pyruvate locks the conforma-tion of the dimer that promotes docking to the moreactive tetrameric form, offering insight into ligand-mediated stabilization of multimeric enzymes.
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000858361 7001_ $$0P:(DE-HGF)0$$aDogovski, Con$$b1
000858361 7001_ $$0P:(DE-HGF)0$$aWood, Kathleen$$b2
000858361 7001_ $$0P:(DE-HGF)0$$aGriffin, Michael D. W.$$b3
000858361 7001_ $$0P:(DE-HGF)0$$aGorman, Michael A.$$b4
000858361 7001_ $$0P:(DE-HGF)0$$aHor, Lilian$$b5
000858361 7001_ $$0P:(DE-HGF)0$$aReboul, Cyril F.$$b6
000858361 7001_ $$0P:(DE-HGF)0$$aBuckle, Ashley M.$$b7
000858361 7001_ $$0P:(DE-Juel1)131044$$aWuttke, Joachim$$b8
000858361 7001_ $$0P:(DE-HGF)0$$aParker, Michael W.$$b9
000858361 7001_ $$0P:(DE-HGF)0$$aDobson, Renwick C. J.$$b10
000858361 7001_ $$0P:(DE-HGF)0$$aPerugini, Matthew A.$$b11$$eCorresponding author
000858361 773__ $$0PERI:(DE-600)2031189-8$$a10.1016/j.str.2018.04.014$$gVol. 26, no. 7, p. 948 - 959.e5$$n7$$p948 - 959.e5$$tStructure$$v26$$x0969-2126$$y2018
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