5A1S
Crystal structure of the sodium-dependent citrate symporter SeCitS form Salmonella enterica.
Summary for 5A1S
| Entry DOI | 10.2210/pdb5a1s/pdb |
| Descriptor | CITRATE-SODIUM SYMPORTER, SODIUM ION, CITRATE ANION, ... (9 entities in total) |
| Functional Keywords | transport protein, membrane protein, symporter, transporter, di-carboxylate transporter |
| Biological source | SALMONELLA ENTERICA |
| Cellular location | Cell membrane : G4BX92 |
| Total number of polymer chains | 4 |
| Total formula weight | 195945.57 |
| Authors | Woehlert, D.,Groetzinger, M.J.,Kuhlbrandt, W.,Yildiz, O. (deposition date: 2015-05-05, release date: 2016-02-17, Last modification date: 2024-05-08) |
| Primary citation | Wohlert, D.,Grotzinger, M.J.,Kuhlbrandt, W.,Yildiz, O. Mechanism of Na(+)-dependent citrate transport from the structure of an asymmetrical CitS dimer. Elife, 4:e09375-e09375, 2015 Cited by PubMed Abstract: The common human pathogen Salmonella enterica takes up citrate as a nutrient via the sodium symporter SeCitS. Uniquely, our 2.5 Å x-ray structure of the SeCitS dimer shows three different conformations of the active protomer. One protomer is in the outside-facing state. Two are in different inside-facing states. All three states resolve the substrates in their respective binding environments. Together with comprehensive functional studies on reconstituted proteoliposomes, the structures explain the transport mechanism in detail. Our results indicate a six-step process, with a rigid-body 31° rotation of a helix bundle that translocates the bound substrates by 16 Å across the membrane. Similar transport mechanisms may apply to a wide variety of related and unrelated secondary transporters, including important drug targets. PubMed: 26636752DOI: 10.7554/eLife.09375 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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