5N9Y
The full-length structure of ZntB
Summary for 5N9Y
| Entry DOI | 10.2210/pdb5n9y/pdb |
| EMDB information | 3605 |
| Descriptor | Zinc transport protein ZntB (1 entity in total) |
| Functional Keywords | zntb, zinc transport, cora, membrane protein |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 5 |
| Total formula weight | 183260.41 |
| Authors | Cornelius, G.,Stetsenko, A.,Scheres, S.H.W.,Slotboom, D.J.,Guskov, A. (deposition date: 2017-02-27, release date: 2017-11-15, Last modification date: 2025-05-07) |
| Primary citation | Gati, C.,Stetsenko, A.,Slotboom, D.J.,Scheres, S.H.W.,Guskov, A. The structural basis of proton driven zinc transport by ZntB. Nat Commun, 8:1313-1313, 2017 Cited by PubMed Abstract: Zinc is an essential microelement to sustain all forms of life. However, excess of zinc is toxic, therefore dedicated import, export and storage proteins for tight regulation of the zinc concentration have evolved. In Enterobacteriaceae, several membrane transporters are involved in zinc homeostasis and linked to virulence. ZntB has been proposed to play a role in the export of zinc, but the transport mechanism of ZntB is poorly understood and based only on experimental characterization of its distant homologue CorA magnesium channel. Here, we report the cryo-electron microscopy structure of full-length ZntB from Escherichia coli together with the results of isothermal titration calorimetry, and radio-ligand uptake and fluorescent transport assays on ZntB reconstituted into liposomes. Our results show that ZntB mediates Zn uptake, stimulated by a pH gradient across the membrane, using a transport mechanism that does not resemble the one proposed for homologous CorA channels. PubMed: 29101379DOI: 10.1038/s41467-017-01483-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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