2fuh
From Proteopedia
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Solution Structure of the UbcH5c/Ub Non-covalent Complex
Overview
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.
About this Structure
2FUH is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
Reference
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
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