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PDBsum entry 1jbb

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Top Page protein Protein-protein interface(s) links
Ligase PDB id
1jbb
Contents
Protein chains
148 a.a. *
Waters ×131
* Residue conservation analysis

References listed in PDB file
Key reference
Title Molecular insights into polyubiquitin chain assembly: crystal structure of the mms2/ubc13 heterodimer.
Authors A.P.Vandemark, R.M.Hofmann, C.Tsui, C.M.Pickart, C.Wolberger.
Ref. Cell, 2001, 105, 711-720. [DOI no: 10.1016/S0092-8674(01)00387-7]
PubMed id 11440714
Abstract
While the signaling properties of ubiquitin depend on the topology of polyubiquitin chains, little is known concerning the molecular basis of specificity in chain assembly and recognition. UEV/Ubc complexes have been implicated in the assembly of Lys63-linked polyubiquitin chains that act as a novel signal in postreplicative DNA repair and I kappa B alpha kinase activation. The crystal structure of the Mms2/Ubc13 heterodimer shows the active site of Ubc13 at the intersection of two channels that are potential binding sites for the two substrate ubiquitins. Mutations that destabilize the heterodimer interface confer a marked UV sensitivity, providing direct evidence that the intact heterodimer is necessary for DNA repair. Selective mutations in the channels suggest a molecular model for specificity in the assembly of Lys63-linked polyubiquitin signals.
Figure 2.
Figure 2. The Mms2/Ubc13 Binding Interface Contains Both Hydrophobic and Polar Surfaces(A) Mms2/Ubc13 heterodimerization interface. Ubc13 is displayed as a surface with Mms2 interface residues in light blue.(B) F8A-Mms2 (light blue) environment showing hydrophobic contacts with Ubc13 residues E55, L56, Y57, and R70 (green). The Ubc13 backbone is shown in green.(C) E55-Ubc13 environment highlighting hydrogen bonds that bridge the interface (black). The Mms2 backbone shown in blue, the Ubc13 backbone in green
Figure 4.
Figure 4. Channels and Interfering MutationsThe heterodimer is shown as a surface. The three channels referred to in the text are colored green and numbered, interfering mutations are shown in blue. Ubc13-Cys87 is shown in yellow. The figure was generated with VMD (Humphrey et al., 1996) and RENDER (Merritt and Bacon, 1997)
The above figures are reprinted by permission from Cell Press: Cell (2001, 105, 711-720) copyright 2001.
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