DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Ji Won | ko |
dc.contributor.author | Kim, Subin | ko |
dc.contributor.author | Kim, Songwon | ko |
dc.contributor.author | Lee, Haerim | ko |
dc.contributor.author | Lee, Jie-Oh | ko |
dc.contributor.author | Jin, Mi Sun | ko |
dc.date.accessioned | 2017-07-04T02:48:17Z | - |
dc.date.available | 2017-07-04T02:48:17Z | - |
dc.date.created | 2017-06-23 | - |
dc.date.created | 2017-06-23 | - |
dc.date.issued | 2017-05 | - |
dc.identifier.citation | SCIENTIFIC REPORTS, v.7, no.2548 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | http://hdl.handle.net/10203/224745 | - |
dc.description.abstract | The sodium-dependent citrate transporter of Klebsiella pneumoniae (KpCitS) belongs to the 2-hydroxycarboxylate transporter (2-HCT) family and allows the cell to use citrate as sole carbon and energy source in anaerobic conditions. Here we present crystal structures of KpCitS in citrate-bound outward-facing, citrate-bound asymmetric, and citrate-free inward-facing state. The structures reveal that the KpCitS dimerization domain remains stationary throughout the transport cycle due to a hydrogen bond network as well as extensive hydrophobic interactions. In contrast, its transport domain undergoes a -35(omicron) rigid-body rotation and a -17 angstrom translocation perpendicular to the membrane to expose the substrate-binding site alternately to either side of the membrane. Furthermore, homology models of two other 2-HCT proteins based on the KpCitS structure offer structural insights into their differences in substrate specificity at a molecular level. On the basis of our results and previous biochemical data, we propose that the activity of the 2-HCT CitS involves an elevator-like movement in which the transport domain itself traverses the lipid bilayer, carrying the substrate into the cell in a sodium-dependent manner. | - |
dc.language | English | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | DEPENDENT CITRATE CARRIER | - |
dc.subject | LACTIC-ACID BACTERIA | - |
dc.subject | NA+/CITRATE TRANSPORTER CITS | - |
dc.subject | INWARD-FACING STATE | - |
dc.subject | KLEBSIELLA-PNEUMONIAE | - |
dc.subject | DICARBOXYLATE TRANSPORTER | - |
dc.subject | ELECTRON CRYSTALLOGRAPHY | - |
dc.subject | ASPARTATE TRANSPORTER | - |
dc.subject | FUNCTIONAL-PROPERTIES | - |
dc.subject | MEMBRANE TOPOLOGY | - |
dc.title | Structural insights into the elevator-like mechanism of the sodium/citrate symporter CitS | - |
dc.type | Article | - |
dc.identifier.wosid | 000402519400012 | - |
dc.identifier.scopusid | 2-s2.0-85019976252 | - |
dc.type.rims | ART | - |
dc.citation.volume | 7 | - |
dc.citation.issue | 2548 | - |
dc.citation.publicationname | SCIENTIFIC REPORTS | - |
dc.identifier.doi | 10.1038/s41598-017-02794-x | - |
dc.contributor.localauthor | Lee, Jie-Oh | - |
dc.contributor.nonIdAuthor | Kim, Subin | - |
dc.contributor.nonIdAuthor | Kim, Songwon | - |
dc.contributor.nonIdAuthor | Lee, Haerim | - |
dc.contributor.nonIdAuthor | Jin, Mi Sun | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | DEPENDENT CITRATE CARRIER | - |
dc.subject.keywordPlus | LACTIC-ACID BACTERIA | - |
dc.subject.keywordPlus | NA+/CITRATE TRANSPORTER CITS | - |
dc.subject.keywordPlus | INWARD-FACING STATE | - |
dc.subject.keywordPlus | KLEBSIELLA-PNEUMONIAE | - |
dc.subject.keywordPlus | DICARBOXYLATE TRANSPORTER | - |
dc.subject.keywordPlus | ELECTRON CRYSTALLOGRAPHY | - |
dc.subject.keywordPlus | ASPARTATE TRANSPORTER | - |
dc.subject.keywordPlus | FUNCTIONAL-PROPERTIES | - |
dc.subject.keywordPlus | MEMBRANE TOPOLOGY | - |
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