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Structure paper

TitleHuman CTP synthase filament structure reveals the active enzyme conformation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 24, Issue 6, Page 507-514, Year 2017
Publish dateMay 1, 2017
AuthorsEric 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 AbstractThe 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 linksNat Struct Mol Biol / PubMed:28459447 / PubMed Central
MethodsEM (helical sym.) / EM (single particle) / X-ray diffraction
Resolution2.7 - 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 / precipitant*YM

ChemComp-MG:
Unknown entry

ChemComp-CTP:
CYTIDINE-5'-TRIPHOSPHATE

ChemComp-MRD:
(4R)-2-METHYLPENTANE-2,4-DIOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-UTP:
URIDINE 5'-TRIPHOSPHATE / UTP*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
  • escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
KeywordsLYASE / PYRIMIDINE BIOSYNTHESIS / ENZYME REGULATION VIA POLYMERIZATION / FEEDBACK INHIBITION / LIGASE / PROTEIN FIBRIL / nucleotide metabolism / enzyme / filament / active / metabolic filament

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