7RTM
Cryo-EM Structure of the Sodium-driven Chloride/Bicarbonate Exchanger NDCBE (SLC4A8)
Summary for 7RTM
| Entry DOI | 10.2210/pdb7rtm/pdb |
| EMDB information | 24683 |
| Descriptor | Electroneutral sodium bicarbonate exchanger 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | ndcbe, sodium-driven chloride/bicarbonate exchanger, cryo-em, membrane protein |
| Biological source | Oryctolagus cuniculus |
| Total number of polymer chains | 2 |
| Total formula weight | 130471.79 |
| Authors | Wang, W.G.,Tsirulnikov, K.,Zhekova, H.,Kayik, G.,Muhammad-Khan, H.,Azimov, R.,Abuladze, N.,Kao, L.,Newman, D.,Noskov, S.Y.,Zhou, Z.H.,Pushkin, A.,Kurtz, I. (deposition date: 2021-08-13, release date: 2021-09-29, Last modification date: 2021-10-06) |
| Primary citation | Wang, W.,Tsirulnikov, K.,Zhekova, H.R.,Kayik, G.,Khan, H.M.,Azimov, R.,Abuladze, N.,Kao, L.,Newman, D.,Noskov, S.Y.,Zhou, Z.H.,Pushkin, A.,Kurtz, I. Cryo-EM structure of the sodium-driven chloride/bicarbonate exchanger NDCBE. Nat Commun, 12:5690-5690, 2021 Cited by PubMed Abstract: SLC4 transporters play significant roles in pH regulation and cellular sodium transport. The previously solved structures of the outward facing (OF) conformation for AE1 (SLC4A1) and NBCe1 (SLC4A4) transporters revealed an identical overall fold despite their different transport modes (chloride/bicarbonate exchange versus sodium-carbonate cotransport). However, the exact mechanism determining the different transport modes in the SLC4 family remains unknown. In this work, we report the cryo-EM 3.4 Å structure of the OF conformation of NDCBE (SLC4A8), which shares transport properties with both AE1 and NBCe1 by mediating the electroneutral exchange of sodium-carbonate with chloride. This structure features a fully resolved extracellular loop 3 and well-defined densities corresponding to sodium and carbonate ions in the tentative substrate binding pocket. Further, we combine computational modeling with functional studies to unravel the molecular determinants involved in NDCBE and SLC4 transport. PubMed: 34584093DOI: 10.1038/s41467-021-25998-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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