Solution structure and interaction surface of the C-terminal domain from p47: A major p97-cofactor involved in SNARE disassembly

Xuemei Yuan, Anthony Shaw, Xiaodong Zhang, Hisao Kondo, John Lally, Paul S. Freemont, Stephen Matthews

Research output: Contribution to journalArticlepeer-review

75 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)255-263
Number of pages9
JournalJournal of Molecular Biology
Volume311
Issue number2
DOIs
Publication statusPublished - Aug 10 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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