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Structure paper

TitleG-actin provides substrate-specificity to eukaryotic initiation factor 2 alpha holophosphatases.
Journal, issue, pagesElife, Vol. 4, Year 2015
Publish dateSep 18, 2014 (structure data deposition date)
AuthorsChen, R. / Rato, C. / Yan, Y. / Crespillo-Casado, A. / Clarke, H.J. / Harding, H.P. / Marciniak, S.J. / Read, R.J. / Ron, D.
External linksElife / PubMed:25774600
MethodsX-ray diffraction
Resolution1.55 - 7.88 Å
Structure data

PDB-4v0u:
The crystal structure of ternary PP1G-PPP1R15B and G-actin complex
Method: X-RAY DIFFRACTION / Resolution: 7.88 Å

PDB-4v0v:
The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-660)
Method: X-RAY DIFFRACTION / Resolution: 1.61 Å

PDB-4v0w:
The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4v0x:
The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-684)
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-LAB:
LATRUNCULIN B / toxin*YM

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

ChemComp-MN:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
  • homo sapiens (human)
  • oryctolagus cuniculus (rabbit)
KeywordsMOTOR PROTEIN/HYDROLASE / MOTOR PROTEIN-HYDROLASE COMPLEX / HYDROLASE/HYDROLASE REGULATOR / HYDROLASE-HYDROLASE REGULATOR COMPLEX

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