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Structure paper

TitleStructural analysis of Rtt106p reveals a DNA-binding role required for heterochromatin silencing
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 4251-4262, Year 2010
Publish dateApr 4, 2009 (structure data deposition date)
AuthorsLiu, Y. / Huang, H. / Zhou, B.O. / Wang, S.S. / Hu, Y. / Li, X. / Liu, J. / Zang, J. / Niu, L. / Wu, J. ...Liu, Y. / Huang, H. / Zhou, B.O. / Wang, S.S. / Hu, Y. / Li, X. / Liu, J. / Zang, J. / Niu, L. / Wu, J. / Zhou, J.Q. / Teng, M. / Shi, Y.
External linksJ. Biol. Chem. / PubMed:20007951
MethodsX-ray diffraction
Resolution2.406 - 3.1 Å
Structure data

PDB-3gyo:
Se-Met Rtt106p
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-3gyp:
Rtt106p
Method: X-RAY DIFFRACTION / Resolution: 2.406 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-CL:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCHAPERONE / histone chaperone / Chromosomal protein / Nucleus / Phosphoprotein / Transcription / Transcription regulation / Transposition

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