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TitleMechanism of ubiquitin ligation and lysine prioritization by a HECT E3.
Journal, issue, pagesElife, Vol. 2, Page e00828-e00828, Year 2013
Publish dateJun 21, 2013 (structure data deposition date)
AuthorsKamadurai, H.B. / Qiu, Y. / Deng, A. / Harrison, J.S. / Macdonald, C. / Actis, M. / Rodrigues, P. / Miller, D.J. / Souphron, J. / Lewis, S.M. ...Kamadurai, H.B. / Qiu, Y. / Deng, A. / Harrison, J.S. / Macdonald, C. / Actis, M. / Rodrigues, P. / Miller, D.J. / Souphron, J. / Lewis, S.M. / Kurinov, I. / Fujii, N. / Hammel, M. / Piper, R. / Kuhlman, B. / Schulman, B.A.
External linksElife / PubMed:23936628
MethodsX-ray diffraction
Resolution3.1 Å
Structure data

PDB-4lcd:
Structure of an Rsp5xUbxSna3 complex: Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • homo sapiens (human)
KeywordsLigase/protein binding / Ligase / E3 / Rsp5 / NEDD4 / Ubiquitin / HECT / Sna3 / thioester / maleimide / crosslink / Ligase-protein binding complex

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