5GLF

Structural insights into the interaction of p97 N-terminal domain and SHP motif in Derlin-1 rhomboid pseudoprotease

Summary for 5GLF

• Entry DOI: 10.2210/pdb5glf/pdb
• Descriptor: Transitional endoplasmic reticulum ATPase, Derlin-1 (3 entities in total)
• Functional Keywords: beta-barrel, atpase, derlin1 shp box ubiquitin, phosphorylation, hydrolase-transport protein complex, hydrolase/transport protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, cytosol : P55072; Endoplasmic reticulum membrane ; Multi- pass membrane protein : Q9BUN8
• Total number of polymer chains: 8
• Total formula weight: 89222.11

Authors

Lim, J.J.,Lee, Y.,Yoon, S.Y.,Ly, T.T.,Kang, J.Y.,Youn, H.-S.,An, J.Y.,Lee, J.-G.,Park, K.R.,Kim, T.G.,Yang, J.K.,Jun, Y.,Eom, S.H. (deposition date: 2016-07-11, release date: 2016-11-09, Last modification date: 2023-11-08)

Primary citation

Lim, J.J.,Lee, Y.,Yoon, S.Y.,Ly, T.T.,Kang, J.Y.,Youn, H.S.,An, J.Y.,Lee, J.G.,Park, K.R.,Kim, T.G.,Yang, J.K.,Jun, Y.,Eom, S.H.
Structural insights into the interaction of human p97 N-terminal domain and SHP motif in Derlin-1 rhomboid pseudoprotease.
FEBS Lett., 590:4402-4413, 2016

PubMed Abstract: The interaction of the rhomboid pseudoprotease Derlin-1 and p97 is crucial for the retrotranslocation of polyubiquitinated substrates in the endoplasmic reticulum-associated degradation pathway. We report a 2.25 Å resolution structure of the p97 N-terminal domain (p97N) in complex with the Derlin-1 SHP motif. Remarkably, the SHP motif adopts a short, antiparallel β-strand that interacts with the β-sheet of p97N-a site distinct from that to which most p97 adaptor proteins bind. Mutational and biochemical analyses contributed to defining the specific interaction, demonstrating the importance of a highly conserved binding pocket on p97N and a signature motif on SHP. Our findings may also provide insights into the interactions between other SHP-containing proteins and p97N.

PubMed: 27714797
DOI: 10.1002/1873-3468.12447

Experimental method

X-RAY DIFFRACTION (2.25 Å)