8e6l | pdb_00008e6l

X-ray structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter D296A mutant in an inward-open, manganese-bound state

spinqualitylabelsall models 8e6l, resolution 3.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8e6l is a 1 chain structure with sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.12Å Ligands: CL, GOL, MN, OLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MNTH_DEIRA H(+)-stimulated, divalent metal cation uptake system. Publication Abstract from PubMed Transporters of the Nramp (Natural resistance-associated macrophage protein) family import divalent transition metal ions into cells of most organisms. By supporting metal homeostasis, Nramps prevent diseases and disorders related to metal insufficiency or overload. Previous studies revealed that Nramps take on a LeuT fold and identified the metal-binding site. We present high-resolution structures of Deinococcus radiodurans (Dra)Nramp in three stable conformations of the transport cycle revealing that global conformational changes are supported by distinct coordination geometries of its physiological substrate, Mn(2+), across conformations, and by conserved networks of polar residues lining the inner and outer gates. In addition, a high-resolution Cd(2+)-bound structure highlights differences in how Cd(2+) and Mn(2+) are coordinated by DraNramp. Complementary metal binding studies using isothermal titration calorimetry with a series of mutated DraNramp proteins indicate that the thermodynamic landscape for binding and transporting physiological metals like Mn(2+) is different and more robust to perturbation than for transporting the toxic Cd(2+) metal. Overall, the affinity measurements and high-resolution structural information on metal substrate binding provide a foundation for understanding the substrate selectivity of essential metal ion transporters like Nramps. High-resolution structures with bound Mn(2+) and Cd(2+) map the metal import pathway in an Nramp transporter.,Ray S, Berry SP, Wilson EA, Zhang CH, Shekhar M, Singharoy A, Gaudet R Elife. 2023 Apr 11;12:e84006. doi: 10.7554/eLife.84006. PMID:37039477 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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