Structural highlights
5a1s is a 4 chain structure with sequence from "bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[G4BX92_SALIN] Uptake of citrate across the boundary membrane with the concomitant uptake of a sodium ion (symport system).[PIRNR:PIRNR005348]
Publication Abstract from PubMed
The common human pathogen Salmonella enterica takes up citrate as a nutrient via the sodium symporter SeCitS. Uniquely, our 2.5 A 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 degrees rotation of a helix bundle that translocates the bound substrates by 16 A across the membrane. Similar transport mechanisms may apply to a wide variety of related and unrelated secondary transporters, including important drug targets.
Mechanism of Na(+)-dependent citrate transport from the structure of an asymmetrical CitS dimer.,Wohlert D, Grotzinger MJ, Kuhlbrandt W, Yildiz O Elife. 2015 Dec 4;4. pii: e09375. doi: 10.7554/eLife.09375. PMID:26636752[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wohlert D, Grotzinger MJ, Kuhlbrandt W, Yildiz O. Mechanism of Na(+)-dependent citrate transport from the structure of an asymmetrical CitS dimer. Elife. 2015 Dec 4;4. pii: e09375. doi: 10.7554/eLife.09375. PMID:26636752 doi:http://dx.doi.org/10.7554/eLife.09375
