Mechanism of the pH-induced conformational change in the sensor domain of the DraK histidine kinase via the E83, E105, and E107 residues

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dc.contributor.authorK J Yeo-
dc.contributor.authorYoung-Soo Hong-
dc.contributor.authorJ G Jee-
dc.contributor.authorJae Kyoung Lee-
dc.contributor.authorHyo Jeong Kim-
dc.contributor.authorJ W Park-
dc.contributor.authorE H Kim-
dc.contributor.authorE Hwang-
dc.contributor.authorSang Yoon Kim-
dc.contributor.authorEun Gyeong Lee-
dc.contributor.authorOh Suk Kwon-
dc.contributor.authorH K Cheong-
dc.date.accessioned2017-04-19T09:55:54Z-
dc.date.available2017-04-19T09:55:54Z-
dc.date.issued2014-
dc.identifier.issn1932-6203-
dc.identifier.uri10.1371/journal.pone.0107168ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12157-
dc.description.abstractThe DraR/DraK two-component system was found to be involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner; however, its function and signaling and sensing mechanisms remain unclear. Here, we describe the solution structure of the extracellular sensor domain of DraK and suggest a mechanism for the pH-dependent conformational change of the protein. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase. A biophysical study demonstrates that the E83, E105, and E107 residues have abnormally high pKa values and that they drive the pH-dependent conformational change for the extracellular sensor domain of DraK. We found that a triple mutant (E83L/E105L/E107A) is pH independent and mimics the low pH structure. An in vivo study showed that DraK is essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock. Our findings suggest that the DraR/DraK two-component system plays an important role in the pH regulation of S. coelicolor growth medium. This study provides a foundation for the regulation and the production of secondary metabolites in Streptomyces.-
dc.publisherPublic Library of Science-
dc.titleMechanism of the pH-induced conformational change in the sensor domain of the DraK histidine kinase via the E83, E105, and E107 residues-
dc.title.alternativeMechanism of the pH-induced conformational change in the sensor domain of the DraK histidine kinase via the E83, E105, and E107 residues-
dc.typeArticle-
dc.citation.titlePLoS One-
dc.citation.number9-
dc.citation.endPagee107168-
dc.citation.startPagee107168-
dc.citation.volume9-
dc.contributor.affiliatedAuthorYoung-Soo Hong-
dc.contributor.affiliatedAuthorJae Kyoung Lee-
dc.contributor.affiliatedAuthorHyo Jeong Kim-
dc.contributor.affiliatedAuthorSang Yoon Kim-
dc.contributor.affiliatedAuthorEun Gyeong Lee-
dc.contributor.affiliatedAuthorOh Suk Kwon-
dc.contributor.alternativeName여권주-
dc.contributor.alternativeName홍영수-
dc.contributor.alternativeName지준구-
dc.contributor.alternativeName이재경-
dc.contributor.alternativeName김효정-
dc.contributor.alternativeName박진완-
dc.contributor.alternativeName김은희-
dc.contributor.alternativeName황은하-
dc.contributor.alternativeName김상윤-
dc.contributor.alternativeName이은경-
dc.contributor.alternativeName권오석-
dc.contributor.alternativeName정해갑-
dc.identifier.bibliographicCitationPLoS One, vol. 9, no. 9, pp. e107168-e107168-
dc.identifier.doi10.1371/journal.pone.0107168-
dc.description.journalClassY-
Appears in Collections:
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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