1ZGU

Solution structure of the human Mms2-Ubiquitin complex

Summary for 1ZGU

• Entry DOI: 10.2210/pdb1zgu/pdb
• Descriptor: Ubiquitin-conjugating enzyme E2 variant 2, Ubiquitin (2 entities in total)
• Functional Keywords: uev domain, ubiquitin binding motif, ligase-signaling protein complex, ligase/signaling protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 24438.94

Authors

Lewis, M.J.,Saltibus, L.F.,Hau, D.D.,Xiao, W.,Spyracopoulos, L. (deposition date: 2005-04-22, release date: 2006-04-04, Last modification date: 2024-05-22)

Primary citation

Lewis, M.J.,Saltibus, L.F.,Hau, D.D.,Xiao, W.,Spyracopoulos, L.
Structural Basis for Non-Covalent Interaction Between Ubiquitin and the Ubiquitin Conjugating Enzyme Variant Human MMS2.
J.Biomol.Nmr, 34:89-100, 2006

PubMed Abstract: Modification of proteins by post-translational covalent attachment of a single, or chain, of ubiquitin molecules serves as a signaling mechanism for a number of regulatory functions in eukaryotic cells. For example, proteins tagged with lysine-63 linked polyubiquitin chains are involved in error-free DNA repair. The catalysis of lysine-63 linked polyubiquitin chains involves the sequential activity of three enzymes (E1, E2, and E3) that ultimately transfer a ubiquitin thiolester intermediate to a protein target. The E2 responsible for catalysis of lysine-63 linked polyubiquitination is a protein heterodimer consisting of a canonical E2 known as Ubc13, and an E2-like protein, or ubiquitin conjugating enzyme variant (UEV), known as Mms2. We have determined the solution structure of the complex formed by human Mms2 and ubiquitin using high resolution, solution state nuclear magnetic resonance (NMR) spectroscopy. The structure of the Mms2-Ub complex provides important insights into the molecular basis underlying the catalysis of lysine-63 linked polyubiquitin chains.

PubMed: 16518696
DOI: 10.1007/s10858-005-5583-6

Experimental method

SOLUTION NMR