9K3Y

Cryo-EM structure of E coli pstSCAB in the resting state

Summary for 9K3Y

• Entry DOI: 10.2210/pdb9k3y/pdb
• EMDB information: 62032
• Descriptor: Phosphate transport system permease protein PstA, Phosphate transport system permease protein PstC, Phosphate import ATP-binding protein PstB (3 entities in total)
• Functional Keywords: abc transporter, phosphate transport, pstscab complex, metal transport
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 4
• Total formula weight: 124605.98

Authors

Chen, Q.F.,Xiao, H. (deposition date: 2024-10-20, release date: 2026-02-18)

Primary citation

Xiao, H.,Li, S.,Qi, R.,Hu, Y.,Jiang, X.,Luo, J.,Wu, J.,Zhang, L.,Xu, S.,Lu, D.,Yang, X.,Chen, Q.,Liu, S.
Molecular mechanism of phosphate import by the bacterial PstSCAB transporter.
Nat Commun, 2026

PubMed Abstract: Inorganic phosphate (Pi) is essential for all living organisms. PstSCAB, a bacterial high-affinity ABC transporter, imports Pi under limiting conditions via five subunits: PstA and PstC forming the transmembrane domain (TMD), periplasmic PstS that switches between free and TMD-docked forms for Pi capture and delivery, and two cytosolic PstB subunits for ATP binding and hydrolysis. Its malfunction affects the virulence of pathogenic bacteria, making it pharmaceutically attractive. However, complete structural pictures of PstSCAB in different states remain lacking. Here, we determine cryo-EM structures of PstSCAB in resting, pretranslocation, and catalytic intermediate states, which reveal that conformational changes in PstS and ATP binding/unbinding in PstB collectively induce rigid-body movements of TMD, generating inward- or outward-facing conformations. In TMD, Pi specificity is determined by positively charged Arg220 (PstA) and Arg237 (PstC). This study advances understanding of bacterial Pi import and supports drug development targeting PstSCAB.

PubMed: 41634007
DOI: 10.1038/s41467-026-69153-1

Experimental method

ELECTRON MICROSCOPY (3 Å)