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Structure paper

TitleTorpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif.
Journal, issue, pagesProtein Sci., Vol. 30, Page 966-981, Year 2021
Publish dateNov 28, 2020 (structure data deposition date)
AuthorsSilman, I. / Shnyrov, V.L. / Ashani, Y. / Roth, E. / Nicolas, A. / Sussman, J.L. / Weiner, L.
External linksProtein Sci. / PubMed:33686648
MethodsX-ray diffraction
Resolution1.85 - 2.65 Å
Structure data

PDB-7b2w:
Torpedo californica acetylcholinesterase complexed with UO2
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-7b38:
Torpedo californica acetylcholinesterase complexed with Mg+2
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-7b8e:
Torpedo californica acetylcholinesterase complexed with Ca+2
Method: X-RAY DIFFRACTION / Resolution: 2.23 Å

Chemicals

ChemComp-IUM:
URANYL (VI) ION

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-GOL:
GLYCEROL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-FWN:
2-[2-(2-ethoxyethoxy)ethoxy]ethanol

ChemComp-CA:
Unknown entry

Source
  • tetronarce californica (Pacific electric ray)
KeywordsHYDROLASE / acetylcholinesterase; ASSAM; differential scanning calorimetry; divalent metal ion; electron paramagnetic resonance; thermal inactivation; Torpedo; 4D motif / 3.1.1.7

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