1zc1
From Proteopedia
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Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
Overview
Ufd1 mediates ubiquitin fusion degradation by association with Npl4 and, Cdc48/p97. The Ufd1-ubiquitin interaction is essential for transfer of, substrates to the proteasome. However, the mechanism and specificity of, ubiquitin recognition by Ufd1 are poorly understood due to the lack of, detailed structural information. Here, we present the solution structure, of yeast Ufd1 N domain and show that it has two distinct binding sites for, mono- and polyubiquitin. The structure exhibits striking similarities to, the Cdc48/p97 N domain. It contains the double-psi beta barrel motif, which is thus identified as a ubiquitin binding domain. Significantly, Ufd1 shows higher affinity toward polyubiquitin than monoubiquitin, attributable to the utilization of separate binding sites with different, affinities. Further studies revealed that the Ufd1-ubiquitin interaction, involves hydrophobic contacts similar to those in well-characterized, ubiquitin binding proteins. Our results provide a structural basis for a, previously proposed synergistic binding of polyubiquitin by Cdc48/p97 and, Ufd1.
About this Structure
1ZC1 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites., Park S, Isaacson R, Kim HT, Silver PA, Wagner G, Structure. 2005 Jul;13(7):995-1005. PMID:16004872
Page seeded by OCA on Wed Nov 21 07:22:36 2007
