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-Structure paper
タイトル | Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump. |
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ジャーナル・号・ページ | Elife, Vol. 9, Year 2020 |
掲載日 | 2020年5月27日 |
著者 | Xin Xu / Huigang Shi / Xiaowen Gong / Pu Chen / Ying Gao / Xinzheng Zhang / Song Xiang / |
PubMed 要旨 | 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. |
リンク | Elife / PubMed:32459174 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 3.9 - 4.403 Å |
構造データ | EMDB-9743, PDB-6iww: PDB-6iva: |
化合物 | ChemComp-LMT: |
由来 |
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キーワード | MEMBRANE PROTEIN / decarboxylase sodium pump / biotin-dependent decarboxylase / sodium pump |