5C1B

p97-delta709-728 in complex with a UFD1-SHP peptide

Summary for 5C1B

• Entry DOI: 10.2210/pdb5c1b/pdb
• Descriptor: Transitional endoplasmic reticulum ATPase, Ubiquitin fusion degradation protein 1 homolog, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (7 entities in total)
• Functional Keywords: aaa atpase, erad, vcp, cdc48, hydrolase
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, cytosol: P55072; Nucleus : Q92890
• Total number of polymer chains: 8
• Total formula weight: 532939.00

Authors

Haenzelmann, P.,Schindelin, H. (deposition date: 2015-06-13, release date: 2016-01-13, Last modification date: 2024-01-10)

Primary citation

Hanzelmann, P.,Schindelin, H.
Characterization of an Additional Binding Surface on the p97 N-Terminal Domain Involved in Bipartite Cofactor Interactions.
Structure, 24:140-147, 2016

PubMed Abstract: The type II AAA ATPase p97 interacts with a large number of cofactors that regulate its function by recruiting it to different cellular pathways. Most of the cofactors interact with the N-terminal (N) domain of p97, either via ubiquitin-like domains or short linear binding motifs. While some linear binding motifs form α helices, another group features short stretches of unstructured hydrophobic sequences as found in the so-called SHP (BS1, binding segment 1) motif. Here we present the crystal structure of a SHP-binding motif in complex with p97, which reveals a so far uncharacterized binding site on the p97 N domain that is different from the conserved binding surface of all other known p97 cofactors. This finding explains how cofactors like UFD1/NPL4 and p47 can utilize a bipartite binding mechanism to interact simultaneously with the same p97 monomer via their ubiquitin-like domain and SHP motif.

PubMed: 26712280
DOI: 10.1016/j.str.2015.10.027

Experimental method

X-RAY DIFFRACTION (3.08 Å)