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6C3I

Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter G45R mutant in an inward occluded state

Summary for 6C3I
Entry DOI10.2210/pdb6c3i/pdb
DescriptorDivalent metal cation transporter MntH, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total)
Functional Keywordsdivalent transition metal transporter, leut-fold, manganese importer, proton-coupled secondary transporter, transport protein
Biological sourceDeinococcus radiodurans R1
Total number of polymer chains2
Total formula weight98186.30
Authors
Zimanyi, C.M.,Bozzi, A.T.,Gaudet, R. (deposition date: 2018-01-09, release date: 2019-02-13, Last modification date: 2023-10-04)
Primary citationBozzi, A.T.,Zimanyi, C.M.,Nicoludis, J.M.,Lee, B.K.,Zhang, C.H.,Gaudet, R.
Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter.
Elife, 8:-, 2019
Cited by
PubMed Abstract: Nramp family transporters-expressed in organisms from bacteria to humans-enable uptake of essential divalent transition metals via an alternating-access mechanism that also involves proton transport. We present high-resolution structures of (Dra)Nramp in multiple conformations to provide a thorough description of the Nramp transport cycle by identifying the key intramolecular rearrangements and changes to the metal coordination sphere. Strikingly, while metal transport requires cycling from outward- to inward-open states, efficient proton transport still occurs in outward-locked (but not inward-locked) DraNramp. We propose a model in which metal and proton enter the transporter via the same external pathway to the binding site, but follow separate routes to the cytoplasm, which could facilitate the co-transport of two cationic species. Our results illustrate the flexibility of the LeuT fold to support a broad range of substrate transport and conformational change mechanisms.
PubMed: 30714568
DOI: 10.7554/eLife.41124
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.95012617657 Å)
Structure validation

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