TY - JOUR
T1 - Structure of the UBA domain of Dsk2p in complex with ubiquitin
T2 - Molecular determinants for ubiquitin recognition
AU - Ohno, Ayako
AU - Jee, Jun Goo
AU - Fujiwara, Kenichiro
AU - Tenno, Takeshi
AU - Goda, Natsuko
AU - Tochio, Hidehito
AU - Kobayashi, Hideki
AU - Hiroaki, Hidekazu
AU - Shirakawa, Masahiro
PY - 2005/4
Y1 - 2005/4
N2 - 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 (Dsk2UBA) 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.
AB - 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 (Dsk2UBA) 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.
UR - http://www.scopus.com/inward/record.url?scp=17044420416&partnerID=8YFLogxK
U2 - 10.1016/j.str.2005.01.011
DO - 10.1016/j.str.2005.01.011
M3 - Article
C2 - 15837191
AN - SCOPUS:17044420416
SN - 0969-2126
VL - 13
SP - 521
EP - 532
JO - Structure
JF - Structure
IS - 4
ER -