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TitleDrosophila CTP synthase can form distinct substrate- and product-bound filaments.
Journal, issue, pagesJ Genet Genomics, Vol. 46, Issue 11, Page 537-545, Year 2019
Publish dateNov 20, 2019
AuthorsXian Zhou / Chen-Jun Guo / Huan-Huan Hu / Jiale Zhong / Qianqian Sun / Dandan Liu / Shuang Zhou / Chia Chun Chang / Ji-Long Liu /
PubMed AbstractIntracellular compartmentation is a key strategy for the functioning of a cell. In 2010, several studies revealed that the metabolic enzyme CTP synthase (CTPS) can form filamentous structures termed ...Intracellular compartmentation is a key strategy for the functioning of a cell. In 2010, several studies revealed that the metabolic enzyme CTP synthase (CTPS) can form filamentous structures termed cytoophidia in prokaryotic and eukaryotic cells. However, recent structural studies showed that CTPS only forms inactive product-bound filaments in bacteria while forming active substrate-bound filaments in eukaryotic cells. In this study, using negative staining and cryo-electron microscopy, we demonstrate that Drosophila CTPS, whether in substrate-bound or product-bound form, can form filaments. Our results challenge the previous model and indicate that substrate-bound and product-bound filaments can coexist in the same species. We speculate that the ability to switch between active and inactive cytoophidia in the same cells provides an additional layer of metabolic regulation.
External linksJ Genet Genomics / PubMed:31902586
MethodsEM (helical sym.) / EM (single particle)
Resolution6.09 - 9.58 Å
Structure data

0840

6l6z

EMDB-0840, PDB-6l6z:
Cryo-EM structure of the Drosophila CTP synthase substrate-bound filament
Method: EM (helical sym.) / Resolution: 6.09 Å

0876

6lfg

EMDB-0876, PDB-6lfg:
Cryo-EM structure of the Drosophila CTP synthase product-bound filament
Method: EM (single particle) / Resolution: 9.58 Å

Source
  • drosophila melanogaster (fruit fly)
KeywordsLIGASE / substrate-bound / filament / product-bound

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