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Structure paper

TitleLipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein
Journal, issue, pagesElife, Vol. 7, Year 2018
Publish dateJul 18, 2018 (structure data deposition date)
AuthorsLiu, X.M. / Yamasaki, A. / Du, X.M. / Coffman, V.C. / Ohsumi, Y. / Nakatogawa, H. / Wu, J.Q. / Noda, N.N. / Du, L.L.
External linksElife / PubMed:30451685
MethodsX-ray diffraction
Resolution2.197 - 2.445 Å
Structure data

PDB-6aaf:
Crystal structure of fission yeast Atg8 complexed with the helical AIM of Hfl1.
Method: X-RAY DIFFRACTION / Resolution: 2.197 Å

PDB-6aag:
Crystal structure of budding yeast Atg8 complexed with the helical AIM of Hfl1.
Method: X-RAY DIFFRACTION / Resolution: 2.445 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • schizosaccharomyces pombe (strain 972 / atcc 24843) (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • saccharomyces cerevisiae (strain yjm789) (yeast)
KeywordsMEMBRANE PROTEIN / vacuole / autophagy / VACUOLE AUTOPHAGY

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