Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter.

Content Provider	Europe PMC
Author	Zhang, Yao Jiang, Yuhan Gao, Kaifu Sui, Dexin Yu, Peixuan Su, Min Wei, Guo-Wei Hu, Jian
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.
Journal	Nature Communications [Nat Commun]
Volume Number	14
DOI	10.1038/s41467-023-36048-4
PubMed Central reference number	PMC9873690
Issue Number	1
PubMed reference number	36693843
e-ISSN	20411723
Language	English
Publisher	Nature Publishing Group
Publisher Date	2023-01-24
Publisher Place	London
Access Restriction	Open
Subject Keyword	X-ray crystallography Metals Ion transport Permeation and transport
Content Type	Text
Resource Type	Article
Subject	Chemistry Biochemistry, Genetics and Molecular Biology Physics and Astronomy