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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
External linksPubMed:28459447 / Publisher's page
MethodsEM (single particle) / EM (helical sym.) / X-ray diffraction
Resolution2.7 - 17 A
Structure data

EMDB-8476:
human CTP synthase 1 - mutant H355A

EMDB-8490:
E. coli CTP synthase CC mutant filament

EMDB-8491:
E. coli CTP synthase CC mutant filament

EMDB-8504:
CryoEM structure of the CTP synthase filament at 4.6 Angstrom resolution

EMDB-8513:
E. coli CTP synthase CC mutant filament (product-bound)

EMDB-8474:
Cryo-EM structure of the human CTP synthase filament

EMDB-8475:
Cryo-EM structure of the E. coli CTP synthase tetramer

PDB-5tkv:
X-RAY CRYSTAL STRUCTURE OF THE "CLOSED" CONFORMATION OF CTP-INHIBITED E. COLI CYTIDINE TRIPHOSPHATE (CTP) SYNTHETASE

PDB-5u03:
Cryo-EM structure of the human CTP synthase filament

PDB-5u05:
Cryo-EM structure of the E. coli CTP synthase tetramer

PDB-5u3c:
CryoEM structure of the CTP synthase filament at 4.6 Angstrom resolution

PDB-5u6r:
E. coli CTP synthase CC mutant filament (product-bound)

Chemicals

ChemComp-GLN:
GLUTAMINE

ChemComp-SO4:
SULFATE ION

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL

ChemComp-MG:
MAGNESIUM ION

ChemComp-CTP:
CYTIDINE-5'-TRIPHOSPHATE

ChemComp-MRD:
(4R)-2-METHYLPENTANE-2,4-DIOL

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE

ChemComp-UTP:
URIDINE 5'-TRIPHOSPHATE

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE

SourceHomo sapiens / human
Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 /
Escherichia coli (strain k12) / bacteria /
KeywordsCTP synthetase / Carbon-Nitrogen Ligases / Cryoelectron Microscopy / Crystallography, X-Ray / Humans / Macromolecular Substances / Models, Molecular / Protein Conformation / Protein Multimerization / LYASE / PYRIMIDINE BIOSYNTHESIS / ENZYME REGULATION VIA POLYMERIZATION / FEEDBACK INHIBITION / LIGASE / PROTEIN FIBRIL / nucleotide metabolism / enzyme / filament / active / metabolic filament

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Oct 4, 2017. Three pioneers of this field were awarded Nobel Prize in Chemistry 2017

Three pioneers of this field were awarded Nobel Prize in Chemistry 2017

  • Jacques Dubochet (University of Lausanne, Switzerland) is a pioneer of ice-embedding method of EM specimen (as known as cryo-EM), Most of 3DEM structures in EMDB and PDB are obtained using his method.
  • Joachim Frank (Columbia University, New York, USA) is a pioneer of single particle reconstruction, which is the most used reconstruction method for 3DEM structures in EMDB and EM entries in PDB. And also, he is a develper of Spider, which is one of the most famous software in this field, and is used for some EM Navigor data (e.g. map projection/slice images).
  • Richard Henderson (MRC Laboratory of Molecular Biology, Cambridge, UK) was determined the first biomolecule structure by EM. The first EM entry in PDB, PDB-1brd is determinedby him.

External links: The 2017 Nobel Prize in Chemistry - Press Release

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