Structural highlights
Function
[A0A0F7JAV8_SALTM] Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.[PIRNR:PIRNR015658] [A0A0D6I9X5_SALTM] Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.[HAMAP-Rule:MF_00404][RuleBase:RU004278]
Publication Abstract from PubMed
The oxaloacetate decarboxylase sodium pump (OAD) is a unique primary-active transporter that utilizes the free energy derived from oxaloacetate decarboxylation for sodium transport across the cell membrane. It is composed of 3 subunits: the alpha subunit catalyzes carboxyl-transfer from oxaloacetate to biotin, the membrane integrated beta subunit catalyzes the subsequent carboxyl-biotin decarboxylation and the coupled sodium transport, the gamma subunit interacts with the alpha and beta subunits and stabilizes the OAD complex. We present here structure of the Salmonella typhimurium OAD betagamma sub-complex. The structure revealed that the beta and gamma subunits form a beta3gamma3 hetero-hexamer with extensive interactions between the subunits and shed light on the OAD holo-enzyme assembly. Structure-guided functional studies provided insights into the sodium binding sites in the beta subunit and the coupling between carboxyl-biotin decarboxylation and sodium transport by the OAD beta subunit.
Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump.,Xu X, Shi H, Gong X, Chen P, Gao Y, Zhang X, Xiang S Elife. 2020 May 27;9. pii: 53853. doi: 10.7554/eLife.53853. PMID:32459174[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu X, Shi H, Gong X, Chen P, Gao Y, Zhang X, Xiang S. Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump. Elife. 2020 May 27;9. pii: 53853. doi: 10.7554/eLife.53853. PMID:32459174 doi:http://dx.doi.org/10.7554/eLife.53853
