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2fuh

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2fuh, 10 NMR models ()
Gene: UBE2D3, UBCH5C (Homo sapiens), Rps27a, Uba80, Ubcep1 (Rattus norvegicus)
Activity: Ubiquitin--protein ligase, with EC number 6.3.2.19
Domains: UBCc, Ubiquitin
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution Structure of the UbcH5c/Ub Non-covalent Complex

Publication Abstract from PubMed

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.

A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination., Brzovic PS, Lissounov A, Christensen DE, Hoyt DW, Klevit RE, Mol Cell. 2006 Mar 17;21(6):873-80. PMID:16543155

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2FUH is a 2 chains structure of sequences from Homo sapiens and Rattus norvegicus. Full experimental information is available from OCA.

Reference

  • Brzovic PS, Lissounov A, Christensen DE, Hoyt DW, Klevit RE. A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol Cell. 2006 Mar 17;21(6):873-80. PMID:16543155 doi:10.1016/j.molcel.2006.02.008

Page seeded by OCA on Wed Feb 18 01:56:21 2009

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