Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Human CTP synthase filament structure reveals the active enzyme conformation.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 24, Issue 6, Page 507-514, Year 2017
Publish date	May 1, 2017
Authors	Eric M Lynch / Derrick R Hicks / Matthew Shepherd / James A Endrizzi / Allison Maker / Jesse M Hansen / Rachael M Barry / Zemer Gitai / Enoch P Baldwin / Justin M Kollman /
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 ...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.
External links	Nat Struct Mol Biol / PubMed:28459447 / PubMed Central
Methods	EM (helical sym.) / EM (single particle) / X-ray diffraction
Resolution	2.7 - 17.0 Å
Structure data	8474 5u03 EMDB-8474, PDB-5u03: Cryo-EM structure of the human CTP synthase filament Method: EM (helical sym.) / Resolution: 6.1 Å 8475 5u05 EMDB-8475, PDB-5u05: Cryo-EM structure of the E. coli CTP synthase tetramer Method: EM (single particle) / Resolution: 7.9 Å EMDB-8476: human CTP synthase 1 - mutant H355A Method: EM (single particle) / Resolution: 17.0 Å EMDB-8490: E. coli CTP synthase CC mutant filament Method: EM (helical sym.) / Resolution: 7.6 Å EMDB-8491: E. coli CTP synthase CC mutant filament Method: EM (helical sym.) / Resolution: 8.6 Å 8504 5u3c EMDB-8504, PDB-5u3c: CryoEM structure of the CTP synthase filament at 4.6 Angstrom resolution Method: EM (helical sym.) / Resolution: 4.6 Å 8513 5u6r EMDB-8513, PDB-5u6r: E. coli CTP synthase CC mutant filament (product-bound) Method: EM (helical sym.) / Resolution: 5.7 Å PDB-5tkv: X-RAY CRYSTAL STRUCTURE OF THE "CLOSED" CONFORMATION OF CTP-INHIBITED E. COLI CYTIDINE TRIPHOSPHATE (CTP) SYNTHETASE Method: X-RAY DIFFRACTION / Resolution: 2.7 Å
Chemicals	ChemComp-GLN: GLUTAMINE ChemComp-SO4: SULFATE ION ChemComp-MPD: (4S)-2-METHYL-2,4-PENTANEDIOL / precipitantYM ChemComp-MG: Unknown entry ChemComp-CTP: CYTIDINE-5'-TRIPHOSPHATE ChemComp-MRD: (4R)-2-METHYLPENTANE-2,4-DIOL / precipitantYM ChemComp-HOH: WATER ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-UTP: URIDINE 5'-TRIPHOSPHATE / UTPYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM
Source	homo sapiens (human) escherichia coli (E. coli) escherichia coli (strain k12) (bacteria)
Keywords	LYASE / PYRIMIDINE BIOSYNTHESIS / ENZYME REGULATION VIA POLYMERIZATION / FEEDBACK INHIBITION / LIGASE / PROTEIN FIBRIL / nucleotide metabolism / enzyme / filament / active / metabolic filament