PXD047999

PXD047999 is an original dataset announced via ProteomeXchange.

Title	Magnesium Transporter MgtA revealed as a Dimeric P-type ATPase
Description	Magnesium (Mg2+) uptake systems are present in all domains of life given the vital role of this ion. Bacteria acquire Mg2+ via conserved Mg2+ channels and transporters. The transporters are required for growth when Mg2+ is limiting or during bacterial pathogenesis, but, despite their significance, there are currently no known structures for these transporters. Here we report the first structure of the Mg2+ transporter MgtA solved by single particle cryo-electron microscopy (cryo-EM). We obtained high resolution structures of both a homodimeric form (2.9 A), the first for a P-type ATPase, and a monomeric form (3.6 A). Each monomer unit of MgtA displays a structural architecture that is similar to other P-type ATPases with a transmembrane domain and two soluble domains. The dimer interface consists of contacts between residues in adjacent soluble nucleotide binding and phosphotransfer regions of the haloacid dehalogenase (HAD) domain. The ATP binding site and consequences of nucleotide binding were characterized by a combination of cryo-EM, molecular dynamics simulations, hydrogen-deuterium exchange mass spectrometry, and mutagenesis. Finally, our structure revealed a Mg2+ ion in the transmembrane segments, which, when combined with sequence conservation and mutagenesis studies, allowed us to propose a model for Mg2+ transport across the lipid bilayer. Our dimeric structures of MgtA also reveal regulatory features that have implications for related P-type ATPases such as the calcium pump SERCA.
HostingRepository	PRIDE
AnnounceDate	2025-04-29
AnnouncementXML	Submission_2025-04-29_13:30:28.003.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Julian Langer
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Eclipse; SYNAPT G2-Si

Revision	Datetime	Status	ChangeLog Entry
0	2023-12-20 05:25:56	ID requested
⏵ 1	2025-04-29 13:30:28	announced

Dataset with its publication pending

submitter keyword: cryo-EM, P-type ATPase, ion translocation, transport, dimer,magnesium, oligomer, membrane protein

Julian D. Langer
contact affiliation	Max-Planck Institute for Biophysics
contact email	julian.langer@biophys.mpg.de
lab head
Julian Langer
contact affiliation	MPIs for Biophysics and Brain Research
contact email	julian.langer@biophys.mpg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD047999
     1. Label: PRIDE project
     2. Name: Magnesium Transporter MgtA revealed as a Dimeric P-type ATPase