TY - JOUR
T1 - Mechanism of ubiquitin recognition by the CUE domain of Vps9p
AU - Prag, Gali
AU - Misra, Saurav
AU - Jones, Eudora A.
AU - Ghirlando, Rodolfo
AU - Davies, Brian A.
AU - Horazdovsky, Bruce F.
AU - Hurley, James H.
N1 - Funding Information:
We thank B. Beach for DNA sequencing, A. Hickman for critical comments on the manuscript, G. Miller and R. Trievel for assistance with data collection, and A. Weissman for discussions. This study was supported in part by NIH grant number GM55301 to B.F.H. and a predoctoral fellowship from the HHMI to B.A.D. We acknowledge use of the SBC-CAT and SER-CAT beamlines at the APS, ANL. Use of the Advanced Photon Source was supported by the U.S. Department of Energy, Basic Energy Sciences, Office of Science, under Contract No.W-31-109-Eng-38.
PY - 2003/5/30
Y1 - 2003/5/30
N2 - Coupling of ubiquitin conjugation to ER degradation (CUE) domains are ∼50 amino acid monoubiquitin binding motifs found in proteins of trafficking and ubiquitination pathways. The 2.3 Å structure of the Vps9p-CUE domain is a dimeric domain-swapped variant of the ubiquitin binding UBA domain. The 1.7 Å structure of the CUE:ubiquitin complex shows that one CUE dimer binds one ubiquitin molecule. The bound CUE dimer is kinked relative to the unbound CUE dimer and wraps around ubiquitin. The CUE monomer contains two ubiquitin binding surfaces on opposite faces of the molecule that cannot bind simultaneously to a single ubiquitin molecule. Dimerization of the CUE domain allows both surfaces to contact a single ubiquitin molecule, providing a mechanism for high-affinity binding to monoubiquitin.
AB - Coupling of ubiquitin conjugation to ER degradation (CUE) domains are ∼50 amino acid monoubiquitin binding motifs found in proteins of trafficking and ubiquitination pathways. The 2.3 Å structure of the Vps9p-CUE domain is a dimeric domain-swapped variant of the ubiquitin binding UBA domain. The 1.7 Å structure of the CUE:ubiquitin complex shows that one CUE dimer binds one ubiquitin molecule. The bound CUE dimer is kinked relative to the unbound CUE dimer and wraps around ubiquitin. The CUE monomer contains two ubiquitin binding surfaces on opposite faces of the molecule that cannot bind simultaneously to a single ubiquitin molecule. Dimerization of the CUE domain allows both surfaces to contact a single ubiquitin molecule, providing a mechanism for high-affinity binding to monoubiquitin.
UR - http://www.scopus.com/inward/record.url?scp=0038820382&partnerID=8YFLogxK
U2 - 10.1016/S0092-8674(03)00364-7
DO - 10.1016/S0092-8674(03)00364-7
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AN - SCOPUS:0038820382
VL - 113
SP - 609
EP - 620
JO - Cell
JF - Cell
SN - 0092-8674
IS - 5
ER -