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| 001 | 858361 | ||
| 005 | 20210129235929.0 | ||
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| 100 | 1 | _ | |a Atkinson, Sarah C. |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Substrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target |
| 260 | _ | _ | |a Cambridge, Mass. |c 2018 |b Cell Press |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Protein 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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| 700 | 1 | _ | |a Hor, Lilian |0 P:(DE-HGF)0 |b 5 |
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| 700 | 1 | _ | |a Buckle, Ashley M. |0 P:(DE-HGF)0 |b 7 |
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| 700 | 1 | _ | |a Dobson, Renwick C. J. |0 P:(DE-HGF)0 |b 10 |
| 700 | 1 | _ | |a Perugini, Matthew A. |0 P:(DE-HGF)0 |b 11 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.str.2018.04.014 |g Vol. 26, no. 7, p. 948 - 959.e5 |0 PERI:(DE-600)2031189-8 |n 7 |p 948 - 959.e5 |t Structure |v 26 |y 2018 |x 0969-2126 |
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