5X4L

Crystal structure of the UBX domain of human UBXD7 in complex with p97 N domain

Summary for 5X4L

• Entry DOI: 10.2210/pdb5x4l/pdb
• Related: 5X3P
• Descriptor: Transitional endoplasmic reticulum ATPase, UBX domain-containing protein 7 (3 entities in total)
• Functional Keywords: ubxd7, p97, hydrolase-protein binding complex, hydrolase/protein binding
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, cytosol: P55072; Nucleus : O94888
• Total number of polymer chains: 4
• Total formula weight: 59692.91

Authors

Jiang, T.,Li, Z.,Wang, Y.,Xu, M. (deposition date: 2017-02-13, release date: 2017-03-22, Last modification date: 2024-10-30)

Primary citation

Li, Z.H.,Wang, Y.,Xu, M.,Jiang, T.
Crystal structures of the UBX domain of human UBXD7 and its complex with p97 ATPase
Biochem. Biophys. Res. Commun., 486:94-100, 2017

PubMed Abstract: In humans, UBXD7 (also called UBXN7), an adaptor of p97 ATPase, can participate in the degradation of misfolded or damaged proteins in the p97-mediated ubiquitin proteasome system (UPS). UBXD7 binds to ubiquitinated substrates via its UBA domain and interacts with p97 N-terminal domain through its UBX domain to recruit p97 or the p97 core complex (p97/NPL4/UFD1). Here, we report the crystal structures of the UBX domain of UBXD7 (UBXD7) at 2.0 Å resolution and its complex with p97 N-terminal domain (p97-UBXD7 complex) at 2.4 Å resolution. A structural analysis and isothermal titration calorimetry results provide detailed molecular basis of interaction between UBXD7 and p97. Moreover, structural superpositions suggest that dimerization of UBXD7 via an intermolecular disulfide bond could interfere with the formation of the p97-UBXD7 complex. Interestingly, UBXD7 may have a cooperative effect on p97 interaction with UFD1. Together, these results provide structural and biochemical insights into the interaction between p97 and UBXD7.

PubMed: 28274878
DOI: 10.1016/j.bbrc.2017.03.005

Experimental method

X-RAY DIFFRACTION (2.402 Å)