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PDBsum entry 1zgu
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Ligase/signaling protein
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PDB id
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1zgu
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References listed in PDB file
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Key reference
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Title
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Structural basis for non-Covalent interaction between ubiquitin and the ubiquitin conjugating enzyme variant human mms2.
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Authors
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M.J.Lewis,
L.F.Saltibus,
D.D.Hau,
W.Xiao,
L.Spyracopoulos.
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Ref.
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J Biomol Nmr, 2006,
34,
89.
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PubMed id
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Abstract
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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.
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