2GMI

Mms2/Ubc13~Ubiquitin

Summary for 2GMI

• Entry DOI: 10.2210/pdb2gmi/pdb
• Descriptor: Ubiquitin-conjugating enzyme E2 13, Ubiquitin-conjugating enzyme variant MMS2, Ubiquitin, ... (4 entities in total)
• Functional Keywords: ubiquitin, ubc13, mms2, e2, uev, ubc13 ubiquitin covalent complex, ligase, human protein
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 3
• Total formula weight: 41487.28

Authors

Wolberger, C.,Eddins, M.J.,Carlile, C.M.,Gomez, K.G.,Pickart, C.M. (deposition date: 2006-04-06, release date: 2006-09-19, Last modification date: 2024-11-06)

Primary citation

Eddins, M.J.,Carlile, C.M.,Gomez, K.M.,Pickart, C.M.,Wolberger, C.
Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation.
Nat.Struct.Mol.Biol., 13:915-920, 2006

PubMed Abstract: Lys63-linked polyubiquitin chains participate in nonproteolytic signaling pathways, including regulation of DNA damage tolerance and NF-kappaB activation. E2 enzymes bound to ubiquitin E2 variants (UEV) are vital in these pathways, synthesizing Lys63-linked polyubiquitin chains, but how these complexes achieve specificity for a particular lysine linkage has been unclear. We have determined the crystal structure of an Mms2-Ubc13-ubiquitin (UEV-E2-Ub) covalent intermediate with donor ubiquitin linked to the active site residue of Ubc13. In the structure, the unexpected binding of a donor ubiquitin of one Mms2-Ubc13-Ub complex to the acceptor-binding site of Mms2-Ubc13 in an adjacent complex allows us to visualize at atomic resolution the molecular determinants of acceptor-ubiquitin binding. The structure reveals the key role of Mms2 in allowing selective insertion of Lys63 into the Ubc13 active site and suggests a molecular model for polyubiquitin chain elongation.

PubMed: 16980971
DOI: 10.1038/nsmb1148

Experimental method

X-RAY DIFFRACTION (2.5 Å)