1wr1
From Proteopedia
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The complex sturcture of Dsk2p UBA with ubiquitin
Overview
The ubiquitin-associated (UBA) domain is one of the most frequently, occurring motifs that recognize ubiquitin tags. Dsk2p, a UBA-containing, protein from Saccharomyces cerevisiae, is involved in the, ubiquitin-proteasome proteolytic pathway and has been implicated in, spindle pole duplication. Here we present the solution structure of the, UBA domain of Dsk2p (Dsk2(UBA)) in complex with ubiquitin. The structure, reveals that the UBA domain uses a mode of ubiquitin recognition that is, similar to that of the CUE domain, another ubiquitin binding motif that, shares low sequence homology but high structural similarity with UBA, domains. These two domains, as well as the structurally unrelated, ubiquitin binding motif UIM, provide a common, crucial recognition site, for ubiquitin, comprising a hydrogen-bonding acceptor for the amide group, of Gly-47, and a methyl group that packs against the hydrophobic pocket of, ubiquitin formed by Leu-8, Ile-44, His-68, and Val-70.
About this Structure
1WR1 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition., Ohno A, Jee J, Fujiwara K, Tenno T, Goda N, Tochio H, Kobayashi H, Hiroaki H, Shirakawa M, Structure. 2005 Apr;13(4):521-32. PMID:15837191
Page seeded by OCA on Wed Nov 21 05:36:50 2007
