6M17

The 2019-nCoV RBD/ACE2-B0AT1 complex

Summary for 6M17

• Entry DOI: 10.2210/pdb6m17/pdb
• EMDB information: 30039
• Descriptor: Sodium-dependent neutral amino acid transporter B(0)AT1, Angiotensin-converting enzyme 2, Spike protein S1, ... (9 entities in total)
• Functional Keywords: 2019-ncov rbd, ace2-b0at1 complex, membrane protein, membrane protein-viral protein complex, membrane protein/viral protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 6
• Total formula weight: 394137.56

Authors

Yan, R.H.,Zhang, Y.Y.,Li, Y.N.,Xia, L.,Guo, Y.Y.,Zhou, Q. (deposition date: 2020-02-24, release date: 2020-03-11, Last modification date: 2024-11-13)

Primary citation

Yan, R.,Zhang, Y.,Li, Y.,Xia, L.,Guo, Y.,Zhou, Q.
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2.
Science, 367:1444-1448, 2020

PubMed Abstract: Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter BAT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-BAT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection.

PubMed: 32132184
DOI: 10.1126/science.abb2762

Experimental method

ELECTRON MICROSCOPY (2.9 Å)