TY - JOUR
T1 - Solution structure and interaction surface of the C-terminal domain from p47
T2 - A major p97-cofactor involved in SNARE disassembly
AU - Yuan, Xuemei
AU - Shaw, Anthony
AU - Zhang, Xiaodong
AU - Kondo, Hisao
AU - Lally, John
AU - Freemont, Paul S.
AU - Matthews, Stephen
N1 - Funding Information:
A.S., X.Z., J.L. and P.S.F. thank the support from the Imperial Cancer Research Fund. H.K. is grateful to the support from the MRC and the Wellcome Trust. S.M. and X.Y. thank the Wellcome Trust and the BBSRC.
PY - 2001/8/10
Y1 - 2001/8/10
N2 - p47 is the major protein identified in complex with the cytosolic AAA ATPase p97. It functions as an essential cofactor of p97-regulated membrane fusion, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of membrane fusion. Here, we report the high-resolution NMR structure of the C-terminal domain from p47. It comprises a UBX domain and a 13 residue long structured N-terminal extension. The UBX domain adopts a characteristic ubiquitin fold with a ββαββαβ secondary structure arrangement. Three hydrophobic residues from the N-terminal extension pack closely against a cleft in the UBX domain. We also identify, for the first time, the p97 interaction surface using NMR chemical shift perturbation studies.
AB - p47 is the major protein identified in complex with the cytosolic AAA ATPase p97. It functions as an essential cofactor of p97-regulated membrane fusion, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of membrane fusion. Here, we report the high-resolution NMR structure of the C-terminal domain from p47. It comprises a UBX domain and a 13 residue long structured N-terminal extension. The UBX domain adopts a characteristic ubiquitin fold with a ββαββαβ secondary structure arrangement. Three hydrophobic residues from the N-terminal extension pack closely against a cleft in the UBX domain. We also identify, for the first time, the p97 interaction surface using NMR chemical shift perturbation studies.
UR - http://www.scopus.com/inward/record.url?scp=0035839113&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035839113&partnerID=8YFLogxK
U2 - 10.1006/jmbi.2001.4864
DO - 10.1006/jmbi.2001.4864
M3 - Article
C2 - 11478859
AN - SCOPUS:0035839113
VL - 311
SP - 255
EP - 263
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 2
ER -