7M1T

Crystal structure of an archaeal CNNM, MtCorB, with C-terminal deletion in complex with Mg2+-ATP

Replaces:  7LJ7

Summary for 7M1T

• Entry DOI: 10.2210/pdb7m1t/pdb
• Related: 7LJ6 7M1U 7MSU
• Descriptor: Hemolysin, contains CBS domains, MAGNESIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: corb, cnnm, duf21, magnesium transporter, membrane protein
• Biological source: Methanoculleus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 79175.25

Authors

Chen, Y.S.,Kozlov, G.,Gehring, K. (deposition date: 2021-03-15, release date: 2021-06-16, Last modification date: 2023-10-18)

Primary citation

Chen, Y.S.,Kozlov, G.,Moeller, B.E.,Rohaim, A.,Fakih, R.,Roux, B.,Burke, J.E.,Gehring, K.
Crystal structure of an archaeal CorB magnesium transporter.
Nat Commun, 12:4028-4028, 2021

PubMed Abstract: CNNM/CorB proteins are a broadly conserved family of integral membrane proteins with close to 90,000 protein sequences known. They are associated with Mg transport but it is not known if they mediate transport themselves or regulate other transporters. Here, we determine the crystal structure of an archaeal CorB protein in two conformations (apo and Mg-ATP bound). The transmembrane DUF21 domain exists in an inward-facing conformation with a Mg ion coordinated by a conserved π-helix. In the absence of Mg-ATP, the CBS-pair domain adopts an elongated dimeric configuration with previously unobserved domain-domain contacts. Hydrogen-deuterium exchange mass spectrometry, analytical ultracentrifugation, and molecular dynamics experiments support a role of the structural rearrangements in mediating Mg-ATP sensing. Lastly, we use an in vitro, liposome-based assay to demonstrate direct Mg transport by CorB proteins. These structural and functional insights provide a framework for understanding function of CNNMs in Mg transport and associated diseases.

PubMed: 34188059
DOI: 10.1038/s41467-021-24282-7

Experimental method

X-RAY DIFFRACTION (3.26 Å)