9FQT

Cryo-EM structure of MmCAT1 bound with FrMLV-RBD in the apo inward-open state

Summary for 9FQT

• Entry DOI: 10.2210/pdb9fqt/pdb
• EMDB information: 50668
• Descriptor: High affinity cationic amino acid transporter 1,Green fluorescent protein, Surface protein, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: mmcat1, frmlv-rbd, slc, viral tropism, membrane protein
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 131427.40

Authors

Ye, M.,Zhou, D.,Pike, A.C.W.,Wang, S.,Wang, D.,Bakshi, S.,Brooke, L.,Williams, E.,Elkins, J.,Stuart, D.I.,Sauer, D.B. (deposition date: 2024-06-17, release date: 2025-07-02, Last modification date: 2026-03-04)

Primary citation

Ye, M.,Liang, Z.,Zhou, D.,Pike, A.C.W.,Wang, S.,Wang, D.,Bakshi, S.,Brooke, L.,Williams, E.P.,Elkins, J.M.,Kessler, B.M.,Stuart, D.I.,Sauer, D.B.
Amino acid and viral binding by the high-affinity Cationic Amino acid Transporter 1 (CAT1) from Mus musculus.
Nat Commun, 2026

PubMed Abstract: Arginine, lysine, and ornithine are critical to several fundamental aspects of organismal physiology, including protein structure and function, the urea cycle, and intracellular signaling. These cationic amino acids are imported by several membrane transporters, most notably the Cationic Amino acid Transporters (CATs) in the SLC7 family. Of these, CAT1 is also the receptor for two orthoretroviruses, and determines the host tropism for these viruses. Here, using a combination of CryoEM and in vitro biochemical techniques, we characterize the substrate recognition and transport of CAT1 from Mus musculus. Further, by determining the structures of MmCAT1 in complex with the receptor binding domain from the Friend Murine Leukemia Virus, we identify the key structural interactions that determine the virus' rodent-specific tropism.

PubMed: 41698924
DOI: 10.1038/s41467-026-69421-0

Experimental method

ELECTRON MICROSCOPY (3.5 Å)