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TitleMolecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 114, Page E9811-E9820, Year 2017
Publish dateMay 9, 2016 (structure data deposition date)
AuthorsAlblova, M. / Smidova, A. / Docekal, V. / Vesely, J. / Herman, P. / Obsilova, V. / Obsil, T.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:29087344
MethodsX-ray diffraction
Resolution2.29 - 3.155 Å
Structure data

PDB-5jta:
Neutral trehalase Nth1 from Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION / Resolution: 2.72 Å

PDB-5m4a:
Neutral trehalase Nth1 from Saccharomyces cerevisiae in complex with trehalose
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-5n6n:
CRYSTAL STRUCTURE OF THE 14-3-3:NEUTRAL TREHALASE NTH1 COMPLEX
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

PDB-5nis:
Neutral trehalase Nth1 from Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION / Resolution: 3.155 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CA:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae s288c (yeast)
KeywordsHYDROLASE / trehalase / glycosidase / neutral trehalase / trehalose / SIGNALING PROTEIN / 14-3-3

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