DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Henna | ko |
dc.contributor.author | Youn, Suk-Jun | ko |
dc.contributor.author | Kim, Seong Ok | ko |
dc.contributor.author | Ko, Junsang | ko |
dc.contributor.author | Lee, Jie-Oh | ko |
dc.contributor.author | Choi, Byong-Seok | ko |
dc.date.accessioned | 2015-07-29T01:37:58Z | - |
dc.date.available | 2015-07-29T01:37:58Z | - |
dc.date.created | 2015-07-21 | - |
dc.date.created | 2015-07-21 | - |
dc.date.created | 2015-07-21 | - |
dc.date.issued | 2015-06 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.290, no.26, pp.16393 - 16402 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/200215 | - |
dc.description.abstract | Background: Cyclic di-AMP inactivates the potassium transport activity of KtrA. Results: Cyclic di-AMP binding to KrtA induced conformational changes. Conclusion: Cyclic di-AMP selectively binds to the KtrA RCK_C domain and signals the inactivation of potassium transport. Significance: The molecular basis for the role of cyclic di-AMP in potassium channel activity was investigated. Although it was only recently identified as a second messenger, c-di-AMP was found to have fundamental importance in numerous bacterial functions such as ion transport. The potassium transporter protein, KtrA, was identified as a c-di-AMP receptor. However, the co-crystallization of c-di-AMP with the protein has not been studied. Here, we determined the crystal structure of the KtrA RCK_C domain in complex with c-di-AMP. The c-di-AMP nucleotide, which adopts a U-shaped conformation, is bound at the dimer interface of RCK_C close to helices 3 and 4. c-di-AMP interacts with KtrA RCK_C mainly by forming hydrogen bonds and hydrophobic interactions. c-di-AMP binding induces the contraction of the dimer, bringing the two monomers of KtrA RCK_C into close proximity. The KtrA RCK_C was able to interact with only c-di-AMP, but not with c-di-GMP, 3,3-cGAMP, ATP, and ADP. The structure of the KtrA RCK_C domain and c-di-AMP complex would expand our understanding about the mechanism of inactivation in Ktr transporters governed by c-di-AMP. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | BACILLUS-SUBTILIS | - |
dc.subject | SIGNAL-TRANSDUCTION | - |
dc.subject | DNA INTEGRITY | - |
dc.subject | GMP | - |
dc.subject | REVEALS | - |
dc.subject | BINDING | - |
dc.subject | SYSTEM | - |
dc.subject | IDENTIFICATION | - |
dc.subject | RECOGNITION | - |
dc.subject | HOMEOSTASIS | - |
dc.title | Structural Studies of Potassium Transport Protein KtrA Regulator of Conductance of K+ (RCK) C Domain in Complex with Cyclic Diadenosine Monophosphate (c-di-AMP) | - |
dc.type | Article | - |
dc.identifier.wosid | 000356930100040 | - |
dc.identifier.scopusid | 2-s2.0-84938725052 | - |
dc.type.rims | ART | - |
dc.citation.volume | 290 | - |
dc.citation.issue | 26 | - |
dc.citation.beginningpage | 16393 | - |
dc.citation.endingpage | 16402 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.identifier.doi | 10.1074/jbc.M115.641340 | - |
dc.contributor.localauthor | Lee, Jie-Oh | - |
dc.contributor.localauthor | Choi, Byong-Seok | - |
dc.contributor.nonIdAuthor | Youn, Suk-Jun | - |
dc.contributor.nonIdAuthor | Ko, Junsang | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | bacterial signal transduction | - |
dc.subject.keywordAuthor | crystal structure | - |
dc.subject.keywordAuthor | cyclic diadenosine monophosphate (c-di-AMP) | - |
dc.subject.keywordAuthor | isothermal titration calorimetry (ITC) | - |
dc.subject.keywordAuthor | potassium transport | - |
dc.subject.keywordAuthor | Staphylococcus aureus (S | - |
dc.subject.keywordAuthor | aureus) | - |
dc.subject.keywordAuthor | bacterial signal transduction | - |
dc.subject.keywordAuthor | crystal structure | - |
dc.subject.keywordAuthor | cyclic diadenosine monophosphate (c-di-AMP) | - |
dc.subject.keywordAuthor | isothermal titration calorimetry (ITC) | - |
dc.subject.keywordAuthor | potassium transport | - |
dc.subject.keywordAuthor | Staphylococcus aureus (S | - |
dc.subject.keywordAuthor | aureus) | - |
dc.subject.keywordPlus | BACILLUS-SUBTILIS | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
dc.subject.keywordPlus | DNA INTEGRITY | - |
dc.subject.keywordPlus | GMP | - |
dc.subject.keywordPlus | REVEALS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | HOMEOSTASIS | - |
dc.subject.keywordPlus | BACILLUS-SUBTILIS | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
dc.subject.keywordPlus | DNA INTEGRITY | - |
dc.subject.keywordPlus | GMP | - |
dc.subject.keywordPlus | REVEALS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | HOMEOSTASIS | - |
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