5GW1

Crystal structure of SNX16 PX-Coiled coil in space group P212121

Summary for 5GW1

• Entry DOI: 10.2210/pdb5gw1/pdb
• Related: 5GW0 5GW8
• Descriptor: Sorting nexin-16 (1 entity in total)
• Functional Keywords: sortin nexin, px domain, endosome sorting, protein transport
• Biological source: Homo sapiens (Human)
• Cellular location: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side: P57768
• Total number of polymer chains: 8
• Total formula weight: 171608.53

Authors

Xu, J.,Liu, J. (deposition date: 2016-09-08, release date: 2017-09-13, Last modification date: 2024-11-06)

Primary citation

Xu, J.,Zhang, L.,Ye, Y.,Shan, Y.,Wan, C.,Wang, J.,Pei, D.,Shu, X.,Liu, J.
SNX16 Regulates the Recycling of E-Cadherin through a Unique Mechanism of Coordinated Membrane and Cargo Binding.
Structure, 25:1251-1263.e5, 2017

PubMed Abstract: E-Cadherin is a major component of adherens junctions on cell surfaces. SNX16 is a unique member of sorting nexins that contains a coiled-coil (CC) domain downstream of the PX domain. We report here that SNX16 regulates the recycling trafficking of E-cadherin. We solved the crystal structure of PX-CC unit of SNX16 and revealed a unique shear shaped homodimer. We identified a novel PI3P binding pocket in SNX16 that consists of both the PX and the CC domains. Surprisingly, we showed that the PPII/α2 loop, which is generally regarded as a membrane insertion loop in PX family proteins, is involved in the E-cadherin binding with SNX16. We then proposed a multivalent membrane binding model for SNX16. Our study postulates a new mechanism for coordinated membrane binding and cargo binding for SNX family proteins in general, and provide novel insights into recycling trafficking of E-cadherin.

PubMed: 28712807
DOI: 10.1016/j.str.2017.06.015

Experimental method

X-RAY DIFFRACTION (3.35 Å)