6IVA
Crystal structure of the S. typhimurium oxaloacetate decarboxylase beta-gamma sub-complex
Summary for 6IVA
| Entry DOI | 10.2210/pdb6iva/pdb |
| Descriptor | Oxaloacetate decarboxylase beta chain, Probable oxaloacetate decarboxylase gamma chain (2 entities in total) |
| Functional Keywords | membrane protein, decarboxylase sodium pump, biotin-dependent decarboxylase |
| Biological source | Salmonella enterica I More |
| Total number of polymer chains | 6 |
| Total formula weight | 168197.49 |
| Authors | |
| Primary citation | 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, 9:-, 2020 Cited by 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 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. PubMed: 32459174DOI: 10.7554/eLife.53853 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.403 Å) |
Structure validation
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