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. Author manuscript; available in PMC: 2014 Mar 1.
Published in final edited form as: Crit Rev Biochem Mol Biol. 2012 Dec 13;48(2):89–97. doi: 10.3109/10409238.2012.742856

Figure 2.

Figure 2

Binding to E3 gp78 G2BR domain allosterically regulates the E2 Ube2g2 active site. The unbound Ube2g2 (PDB entry 2CYX) is superimposed on the Ube2g2-gp78 complex. The unbound and bound Ube2g2 structures are shown in yellow and blue, respectively. The gp78 G2BR domain is shown in red. The catalytic site Cys89 is shown in green. Large conformational changes of the loops surround Cys89, including residue Tyr103 (shown in yellow and blue), are induced by E3 binding