5U3C
CryoEM structure of the CTP synthase filament at 4.6 Angstrom resolution
Summary for 5U3C
| Entry DOI | 10.2210/pdb5u3c/pdb |
| Related | 5U6R |
| EMDB information | 8504 8513 |
| Descriptor | CTP synthase, CYTIDINE-5'-TRIPHOSPHATE, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | nucleotide metabolism, metabolic filament, protein fibril, ligase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 245429.35 |
| Authors | Kollman, J.M.,Lynch, E.M. (deposition date: 2016-12-01, release date: 2017-04-26, Last modification date: 2024-11-20) |
| Primary citation | Lynch, E.M.,Hicks, D.R.,Shepherd, M.,Endrizzi, J.A.,Maker, A.,Hansen, J.M.,Barry, R.M.,Gitai, Z.,Baldwin, E.P.,Kollman, J.M. Human CTP synthase filament structure reveals the active enzyme conformation. Nat. Struct. Mol. Biol., 24:507-514, 2017 Cited by PubMed Abstract: The universally conserved enzyme CTP synthase (CTPS) forms filaments in bacteria and eukaryotes. In bacteria, polymerization inhibits CTPS activity and is required for nucleotide homeostasis. Here we show that for human CTPS, polymerization increases catalytic activity. The cryo-EM structures of bacterial and human CTPS filaments differ considerably in overall architecture and in the conformation of the CTPS protomer, explaining the divergent consequences of polymerization on activity. The structure of human CTPS filament, the first structure of the full-length human enzyme, reveals a novel active conformation. The filament structures elucidate allosteric mechanisms of assembly and regulation that rely on a conserved conformational equilibrium. The findings may provide a mechanism for increasing human CTPS activity in response to metabolic state and challenge the assumption that metabolic filaments are generally storage forms of inactive enzymes. Allosteric regulation of CTPS polymerization by ligands likely represents a fundamental mechanism underlying assembly of other metabolic filaments. PubMed: 28459447DOI: 10.1038/nsmb.3407 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.6 Å) |
Structure validation
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