8ABQ

Structure of the SNX1-SNX5 complex, Pt derivative

Summary for 8ABQ

• Entry DOI: 10.2210/pdb8abq/pdb
• Related: 8A1G
• Descriptor: Sorting nexin-1, Sorting nexin-5, PLATINUM (II) ION, ... (4 entities in total)
• Functional Keywords: snx, membrane trafficking, transport protein, protein transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 103645.37

Authors

Lopez-Robles, C.,Scaramuzza, S.,Astorga-Simon, E.N.,Banos-Mateos, S.,Vidaurrazaga, A.,Rojas, A.L.,Castano, D.,Hierro, A. (deposition date: 2022-07-04, release date: 2023-06-21, Last modification date: 2024-06-19)

Primary citation

Lopez-Robles, C.,Scaramuzza, S.,Astorga-Simon, E.N.,Ishida, M.,Williamson, C.D.,Banos-Mateos, S.,Gil-Carton, D.,Romero-Durana, M.,Vidaurrazaga, A.,Fernandez-Recio, J.,Rojas, A.L.,Bonifacino, J.S.,Castano-Diez, D.,Hierro, A.
Architecture of the ESCPE-1 membrane coat.
Nat.Struct.Mol.Biol., 30:958-969, 2023

PubMed Abstract: Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1), which rescues transmembrane proteins from the endolysosomal pathway for transport to the trans-Golgi network and the plasma membrane. This rescue entails the formation of recycling tubules through ESCPE-1 recruitment, cargo capture, coat assembly and membrane sculpting by mechanisms that remain largely unknown. Herein, we show that ESCPE-1 has a single-layer coat organization and suggest how synergistic interactions between ESCPE-1 protomers, phosphoinositides and cargo molecules result in a global arrangement of amphipathic helices to drive tubule formation. Our results thus define a key process of tubule-based endosomal sorting.

PubMed: 37322239
DOI: 10.1038/s41594-023-01014-7

Experimental method

X-RAY DIFFRACTION (2.81 Å)