7msu | pdb_00007msu

Crystal structure of an archaeal CNNM, MtCorB, CBS-pair domain in complex with Mg2+-ATP

spinqualitylabelsall models 7msu, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7msu is a 1 chain structure with sequence from Atcc 33837. This structure supersedes the now removed PDB entry 7lj6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, EDO, MG Related: 7m1t, 7m1u Gene: SAMN04488571_101329 (ATCC 33837) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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(2+) 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(2+)-ATP bound). The transmembrane DUF21 domain exists in an inward-facing conformation with a Mg(2+) ion coordinated by a conserved pi-helix. In the absence of Mg(2+)-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(2+)-ATP sensing. Lastly, we use an in vitro, liposome-based assay to demonstrate direct Mg(2+) transport by CorB proteins. These structural and functional insights provide a framework for understanding function of CNNMs in Mg(2+) transport and associated diseases. Crystal structure of an archaeal CorB magnesium transporter.,Chen YS, Kozlov G, Moeller BE, Rohaim A, Fakih R, Roux B, Burke JE, Gehring K Nat Commun. 2021 Jun 29;12(1):4028. doi: 10.1038/s41467-021-24282-7. PMID:34188059 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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