Evidence map›Paper›PMID 39516201›Full record

ArticleNature communications2024

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

Yao Zhang, Majid Jafari, Tuo Zhang, Dexin Sui, Luca Sagresti, Kenneth M Merz, Jian Hu

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Yao Zhang *Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA.ORCID 0000-0002-7017-3586
Majid Jafari *Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA.
Tuo Zhang *Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA.ORCID 0000-0002-0900-9285
Dexin SuiDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA.
Luca SagrestiScuola Normale Superiore, Pisa, Italy.ORCID 0000-0001-8379-3170
Kenneth M MerzDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA. merz@chemistry.msu.edu.ORCID 0000-0001-9139-5893
Jian HuDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA. hujian1@msu.edu.ORCID 0000-0001-6657-9826

Funding

Modeling Transition Metal Ion Binding to ProteinsR01GM130641 · NIGMS · MICHIGAN STATE UNIVERSITY · PI KENNETH M. MERZ · 2019 to 2026
$2.5M
Transport, substrate specificity and regulation mechanisms of the ZIP transition metal transportersR35GM140931 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HU, JIAN · 2021 to 2025
$1.7M
Structural and Mechanistic Characterization of the ZIP Metal TransportersR01GM129004 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HU, JIAN · 2018 to 2020
$593k
Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) GM130641Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) GM140931NIGMS NIH HHS R01 GM129004NIGMS NIH HHS R01 GM130641NIGMS NIH HHS R35 GM140931
6 · The paper itself

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.

Indexed as

Bacterial ProteinsBinding SitesBiological TransportBordetella bronchisepticaCation Transport ProteinsCrystallography, X-RayModels, MolecularProtein ConformationZincBacterial ProteinsCation Transport ProteinsZinc

Identifiers

PMID39516201
PMCPMC11549095

What Socratic holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.