期刊
Nature Communications
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12163
关键词
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资金
- BBSRC [BB/L015048/1, BB/K017802/1, BB/H013636/1]
- BBSRC/EPSRC-funded Manchester Synthetic Biology Research Centre, SYNBIOCHEM [BB/M017702/1]
- British Mass Spectrometry Society
- Biotechnology and Biological Sciences Research Council [BB/L015048/1, 1733990, 1498981, BB/H013636/1, BB/K017802/1, BB/L002655/1, BB/M017702/1] Funding Source: researchfish
- BBSRC [BB/K017802/1, BB/L002655/1, BB/L015048/1, BB/M017702/1, BB/H013636/1] Funding Source: UKRI
Fdc1 is a decarboxylase enzyme that requires the novel prenylated FMN cofactor for activity. Here, we use it as an exemplar system to show how native top-down and bottom-up mass spectrometry can measure the structural effect of cofactor binding by a protein. For Fdc1(Ubix), the cofactor confers structural stability to the enzyme. IM-MS shows the holo protein to exist in four closely related conformational families, the populations of which differ in the apo form; the two smaller families are more populated in the presence of the cofactor and depopulated in its absence. These findings, supported by MD simulations, indicate a more open structure for the apo form. HDX-MS reveals that while the dominant structural changes occur proximal to the cofactor-binding site, rearrangements on cofactor binding are evident throughout the protein, predominantly attributable to allosteric conformational tightening, consistent with IM-MS data.
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