6D91
Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter in the outward-open, apo conformation
Summary for 6D91
| Entry DOI | 10.2210/pdb6d91/pdb |
| Descriptor | Divalent metal cation transporter MntH, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total) |
| Functional Keywords | divalent transition metal transporter, leut-fold, manganese importer, proton-coupled secondary transporter, transport protein |
| Biological source | Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 |
| Total number of polymer chains | 1 |
| Total formula weight | 46751.11 |
| Authors | Bozzi, A.T.,Zimanyi, C.M.,Nicoludis, J.M.,Gaudet, R. (deposition date: 2018-04-27, release date: 2019-02-13, Last modification date: 2024-12-25) |
| Primary citation | Bozzi, 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: 30714568DOI: 10.7554/eLife.41124 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.356 Å) |
Structure validation
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