5WY2

Human Snx5 PX domain in complex with Chlamydia IncE C terminus

Summary for 5WY2

• Entry DOI: 10.2210/pdb5wy2/pdb
• Descriptor: Sorting nexin-5, IncE (3 entities in total)
• Functional Keywords: complex, ince, px domain, snx5, transport protein-unknown function complex, transport protein/unknown function
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 41610.80

Authors

Sun, Q.,Yong, X.,Jia, D. (deposition date: 2017-01-10, release date: 2017-11-22, Last modification date: 2023-11-22)

Primary citation

Sun, Q.,Yong, X.,Sun, X.,Yang, F.,Dai, Z.,Gong, Y.,Zhou, L.,Zhang, X.,Niu, D.,Dai, L.,Liu, J.J.,Jia, D.
Structural and functional insights into sorting nexin 5/6 interaction with bacterial effector IncE.
Signal Transduct Target Ther, 2:17030-17030, 2017

PubMed Abstract: The endosomal trafficking pathways are essential for many cellular activities. They are also important targets by many intracellular pathogens. Key regulators of the endosomal trafficking include the retromer complex and sorting nexins (SNXs). effector protein IncE directly targets the retromer components SNX5 and SNX6 and suppresses retromer-mediated transport, but the exact mechanism has remained unclear. We present the crystal structure of the PX domain of SNX5 in complex with IncE, showing that IncE binds to a highly conserved hydrophobic groove of SNX5. The unique helical hairpin of SNX5/6 is essential for binding, explaining the specificity of SNX5/6 for IncE. The SNX5/6-IncE interaction is required for cellular localization of IncE and its inhibitory function. Mechanistically, IncE inhibits the association of CI-MPR cargo with retromer-containing endosomal subdomains. Our study provides new insights into the regulation of retromer-mediated transport and illustrates the intricate competition between host and pathogens in controlling cellular trafficking.

PubMed: 29263922
DOI: 10.1038/sigtrans.2017.30

Experimental method

X-RAY DIFFRACTION (1.9 Å)