6KSW

Cryo-EM structure of the human concentrative nucleoside transporter CNT3

Summary for 6KSW

• Entry DOI: 10.2210/pdb6ksw/pdb
• EMDB information: 0775
• Descriptor: Solute carrier family 28 member 3 (1 entity in total)
• Functional Keywords: nucleoside, trimer, sodium symporter, slc, transport protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 3
• Total formula weight: 211110.33

Authors

Zhou, Y.X.,Liao, L.H.,Li, J.L.,Xiao, Q.J.,Sun, L.F.,Deng, D. (deposition date: 2019-08-26, release date: 2020-08-26, Last modification date: 2024-03-27)

Primary citation

Zhou, Y.X.,Liao, L.H.,Wang, C.,Li, J.L.,Chi, P.,Xiao, Q.J.,Liu, Q.,Guo, L.,Sun, L.F.,Deng, D.
Cryo-EM structure of the human concentrative nucleoside transporter CNT3.
Plos Biol., 18:e3000790-e3000790, 2020

PubMed Abstract: Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs.

PubMed: 32776918
DOI: 10.1371/journal.pbio.3000790

Experimental method

ELECTRON MICROSCOPY (3.6 Å)