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TitleAllosteric regulation of E2:E3 interactions promote a processive ubiquitination machine.
Journal, issue, pagesEmbo J., Vol. 32, Page 2504-2516, Year 2013
Publish dateAug 27, 2012 (structure data deposition date)
AuthorsDas, R. / Liang, Y.H. / Mariano, J. / Li, J. / Huang, T. / King, A. / Tarasov, S.G. / Weissman, A.M. / Ji, X. / Byrd, R.A.
External linksEmbo J. / PubMed:23942235
MethodsNMR (solution) / X-ray diffraction
Resolution2.3 Å
Structure data

PDB-2lxh:
NMR structure of the RING domain in ubiquitin ligase gp78
Method: SOLUTION NMR

PDB-2lxp:
NMR structure of two domains in ubiquitin ligase gp78, RING and G2BR, bound to its conjugating enzyme Ube2g
Method: SOLUTION NMR

PDB-4lad:
Crystal Structure of the Ube2g2:RING-G2BR complex
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-OXL:
OXALATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE / RING domain / ubiquitin / LIGASE/LIGASE / E2:E3 complex / LIGASE-LIGASE complex

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