1WR1

The complex structure of Dsk2p UBA with ubiquitin

Summary for 1WR1

• Entry DOI: 10.2210/pdb1wr1/pdb
• Related: 1D3Z
• Descriptor: Ubiquitin, Ubiquitin-like protein DSK2 (2 entities in total)
• Functional Keywords: uba domain, uba-ubiquitin complex, dsk2, signaling protein
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 14750.51

Authors

Ohno, A.,Jee, J.G.,Fujiwara, K.,Tenno, T.,Goda, N.,Tochio, H.,Hiroaki, H.,kobayashi, H.,Shirakawa, M. (deposition date: 2004-10-08, release date: 2005-04-19, Last modification date: 2023-09-27)

Primary citation

Ohno, A.,Jee, J.,Fujiwara, K.,Tenno, T.,Goda, N.,Tochio, H.,Kobayashi, H.,Hiroaki, H.,Shirakawa, M.
Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition.
Structure, 13:521-532, 2005

PubMed Abstract: 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.

PubMed: 15837191
DOI: 10.1016/j.str.2005.01.011

Experimental method

SOLUTION NMR