5JHO
Crystal structure of the regulatory domain of the sodium driven chloride bicarbonate exchanger.
Summary for 5JHO
| Entry DOI | 10.2210/pdb5jho/pdb |
| Descriptor | Electroneutral sodium bicarbonate exchanger 1 (2 entities in total) |
| Functional Keywords | membrane protein, bicarbonate exchanger, anion transport, transport protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Membrane ; Multi-pass membrane protein : Q2Y0W8 |
| Total number of polymer chains | 2 |
| Total formula weight | 77812.02 |
| Authors | Alvadia, C.,Sommer, T.,Bjerregaard-Andersen, K.,Morth, J.P. (deposition date: 2016-04-21, release date: 2017-08-16, Last modification date: 2024-05-08) |
| Primary citation | Alvadia, C.M.,Sommer, T.,Bjerregaard-Andersen, K.,Damkier, H.H.,Montrasio, M.,Aalkjaer, C.,Morth, J.P. The crystal structure of the regulatory domain of the human sodium-driven chloride/bicarbonate exchanger. Sci Rep, 7:12131-12131, 2017 Cited by PubMed Abstract: The sodium-driven chloride/bicarbonate exchanger (NDCBE) is essential for maintaining homeostatic pH in neurons. The crystal structure at 2.8 Å resolution of the regulatory N-terminal domain of human NDCBE represents the first crystal structure of an electroneutral sodium-bicarbonate cotransporter. The crystal structure forms an equivalent dimeric interface as observed for the cytoplasmic domain of Band 3, and thus establishes that the consensus motif VTVLP is the key minimal dimerization motif. The VTVLP motif is highly conserved and likely to be the physiologically relevant interface for all other members of the SLC4 family. A novel conserved Zn-binding motif present in the N-terminal domain of NDCBE is identified and characterized in vitro. Cellular studies confirm the Zn dependent transport of two electroneutral bicarbonate transporters, NCBE and NBCn1. The Zn site is mapped to a cluster of histidines close to the conserved ETARWLKFEE motif and likely plays a role in the regulation of this important motif. The combined structural and bioinformatics analysis provides a model that predicts with additional confidence the physiologically relevant interface between the cytoplasmic domain and the transmembrane domain. PubMed: 28935959DOI: 10.1038/s41598-017-12409-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.801 Å) |
Structure validation
Download full validation report
