2gmi

OverviewOverview

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.

About this StructureAbout this Structure

2GMI is a Protein complex structure of sequences from Homo sapiens and Saccharomyces cerevisiae. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.

ReferenceReference

Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation., Eddins MJ, Carlile CM, Gomez KM, Pickart CM, Wolberger C, Nat Struct Mol Biol. 2006 Oct;13(10):915-20. Epub 2006 Sep 17. PMID:16980971

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