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Title | Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump. |
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Journal, issue, pages | Elife, Vol. 9, Year 2020 |
Publish date | May 27, 2020 |
![]() | Xin Xu / Huigang Shi / Xiaowen Gong / Pu Chen / Ying Gao / Xinzheng Zhang / Song Xiang / ![]() |
PubMed Abstract | 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 ...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 α subunit catalyzes carboxyl-transfer from oxaloacetate to biotin, the membrane integrated β subunit catalyzes the subsequent carboxyl-biotin decarboxylation and the coupled sodium transport, the γ subunit interacts with the α and β subunits and stabilizes the OAD complex. We present here structure of the OAD βγ sub-complex. The structure revealed that the β and γ subunits form a βγ 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 β subunit and the coupling between carboxyl-biotin decarboxylation and sodium transport by the OAD β subunit. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.9 - 4.403 Å |
Structure data | EMDB-9743, PDB-6iww: ![]() PDB-6iva: |
Chemicals | ![]() ChemComp-LMT: |
Source |
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![]() | MEMBRANE PROTEIN / decarboxylase sodium pump / biotin-dependent decarboxylase / sodium pump |