Molecular insights into substrate translocation in an elevator-type metal transporter

Yao Zhang, Majid Jafari, Tuo Zhang, Dexin Sui, Luca Sagresti, Kenneth M. Merz () and Jian Hu ()
Additional contact information
Yao Zhang: Michigan State University
Majid Jafari: Michigan State University
Tuo Zhang: Michigan State University
Dexin Sui: Michigan State University
Luca Sagresti: Scuola Normale Superiore
Kenneth M. Merz: Michigan State University
Jian Hu: Michigan State University

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract The Zrt/Irt-like protein (ZIP) metal transporters are key players in maintaining the homeostasis of a panel of essential microelements. The prototypical ZIP from Bordetella bronchiseptica (BbZIP) is an elevator transporter, but how the metal substrate moves along the transport pathway and how the transporter changes conformation to allow alternating access remain to be elucidated. Here, we combine structural, biochemical, and computational approaches to investigate the process of metal substrate translocation along with the global structural rearrangement. Our study reveals an upward hinge motion of the transport domain in a high-resolution crystal structure of a cross-linked variant, elucidates the mechanisms of metal release from the transport site into the cytoplasm and activity regulation by a cytoplasmic metal-binding loop, and unravels an unusual elevator mode in enhanced sampling simulations that distinguishes BbZIP from other elevator transporters. This work provides important insights into the metal transport mechanism of the ZIP family.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-54048-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54048-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-54048-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().