2FUH

Solution Structure of the UbcH5c/Ub Non-covalent Complex

Summary for 2FUH

• Entry DOI: 10.2210/pdb2fuh/pdb
• Descriptor: Ubiquitin-conjugating enzyme E2 D3, Ubiquitin (2 entities in total)
• Functional Keywords: protein-protein complex ubiquitin ubiquitin-conjugating enzyme, ligase
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Peripheral membrane protein: P61077
• Total number of polymer chains: 2
• Total formula weight: 25151.77

Authors

Brzovic, P.S.,Lissounov, A.,Hoyt, D.W.,Klevit, R.E. (deposition date: 2006-01-26, release date: 2006-03-28, Last modification date: 2024-05-29)

Primary citation

Brzovic, P.S.,Lissounov, A.,Christensen, D.E.,Hoyt, D.W.,Klevit, R.E.
A UbcH5/Ubiquitin Noncovalent Complex Is Required for Processive BRCA1-Directed Ubiquitination.
Mol.Cell, 21:873-880, 2006

PubMed Abstract: Protein ubiquitination is a powerful regulatory modification that influences nearly every aspect of eukaryotic cell biology. The general pathway for ubiquitin (Ub) modification requires the sequential activities of a Ub-activating enzyme (E1), a Ub transfer enzyme (E2), and a Ub ligase (E3). The E2 must recognize both the E1 and a cognate E3 in addition to carrying activated Ub. These central functions are performed by a topologically conserved alpha/beta-fold core domain of approximately 150 residues shared by all E2s. However, as presented herein, the UbcH5 family of E2s can also bind Ub noncovalently on a surface well removed from the E2 active site. We present the solution structure of the UbcH5c/Ub noncovalent complex and demonstrate that this noncovalent interaction permits self-assembly of activated UbcH5c approximately Ub molecules. Self-assembly has profound consequences for the processive formation of polyubiquitin (poly-Ub) chains in ubiquitination reactions directed by the breast and ovarian cancer tumor susceptibility protein BRCA1.

PubMed: 16543155
DOI: 10.1016/j.molcel.2006.02.008

Experimental method

SOLUTION NMR