8CZJ

A bacteria Zrt/Irt-like protein in the apo state

Summary for 8CZJ

• Entry DOI: 10.2210/pdb8czj/pdb
• Descriptor: Putative membrane protein, SULFATE ION, [(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate, ... (4 entities in total)
• Functional Keywords: transport protein
• Biological source: Bordetella bronchiseptica RB50
• Total number of polymer chains: 2
• Total formula weight: 65995.95

Authors

Zhang, Y.,Hu, J. (deposition date: 2022-05-24, release date: 2023-02-22, Last modification date: 2024-03-06)

Primary citation

Zhang, Y.,Jiang, Y.,Gao, K.,Sui, D.,Yu, P.,Su, M.,Wei, G.W.,Hu, J.
Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter.
Nat Commun, 14:385-385, 2023

PubMed Abstract: The Zrt-/Irt-like protein (ZIP) family consists of ubiquitously expressed divalent metal transporters critically involved in maintaining systemic and cellular homeostasis of zinc, iron, and manganese. Here, we present a study on a prokaryotic ZIP from Bordetella bronchiseptica (BbZIP) by combining structural biology, evolutionary covariance, computational modeling, and a variety of biochemical assays to tackle the issue of the transport mechanism which has not been established for the ZIP family. The apo state structure in an inward-facing conformation revealed a disassembled transport site, altered inter-helical interactions, and importantly, a rigid body movement of a 4-transmembrane helix (TM) bundle relative to the other TMs. The computationally generated and biochemically validated outward-facing conformation model revealed a slide of the 4-TM bundle, which carries the transport site(s), by approximately 8 Å toward the extracellular side against the static TMs which mediate dimerization. These findings allow us to conclude that BbZIP is an elevator-type transporter.

PubMed: 36693843
DOI: 10.1038/s41467-023-36048-4

Experimental method

X-RAY DIFFRACTION (2.751 Å)