1J74

Crystal Structure of Mms2

Summary for 1J74

• Entry DOI: 10.2210/pdb1j74/pdb
• Descriptor: MMS2 (2 entities in total)
• Functional Keywords: mms2, uev, ubiquitin, ubc, dna repair, unknown function
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 16380.73

Authors

Moraes, T.F.,Edwards, R.A.,McKenna, S.,Pastushok, L.,Xiao, W.,Glover, J.N.M.,Ellison, M.J. (deposition date: 2001-05-15, release date: 2001-08-08, Last modification date: 2023-08-16)

Primary citation

Moraes, T.F.,Edwards, R.A.,McKenna, S.,Pastushok, L.,Xiao, W.,Glover, J.N.,Ellison, M.J.
Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13.
Nat.Struct.Biol., 8:669-673, 2001

PubMed Abstract: The ubiquitin conjugating enzyme complex Mms2-Ubc13 plays a key role in post-replicative DNA repair in yeast and the NF-kappaB signal transduction pathway in humans. This complex assembles novel polyubiquitin chains onto yet uncharacterized protein targets. Here we report the crystal structure of a complex between hMms2 (Uev1) and hUbc13 at 1.85 A resolution and a structure of free hMms2 at 1.9 A resolution. These structures reveal that the hMms2 monomer undergoes a localized conformational change upon interaction with hUbc13. The nature of the interface provides a physical basis for the preference of Mms2 for Ubc13 as a partner over a variety of other structurally similar ubiquitin-conjugating enzymes. The structure of the hMms2-hUbc13 complex provides the conceptual foundation for understanding the mechanism of Lys 63 multiubiquitin chain assembly and for its interactions with the RING finger proteins Rad5 and Traf6.

PubMed: 11473255
DOI: 10.1038/90373

Experimental method

X-RAY DIFFRACTION (1.9 Å)