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dc.contributor.authorLuo, Shih-Chien_US
dc.contributor.authorLou, Yuan-Chaoen_US
dc.contributor.authorCheng, Hsin-Yaoen_US
dc.contributor.authorPan, Yun-Ruen_US
dc.contributor.authorPeng, Hwei-Lingen_US
dc.contributor.authorChen, Chinpanen_US
dc.date.accessioned2014-12-08T15:38:24Z-
dc.date.available2014-12-08T15:38:24Z-
dc.date.issued2010-12-01en_US
dc.identifier.issn1047-8477en_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.jsb.2010.06.007en_US
dc.identifier.urihttp://hdl.handle.net/11536/26284-
dc.description.abstractIn bacteria, the two-component system (TCS) is the most prevalent for sensing and transducing the environmental signals into the cell. In Salmonella, the small basic protein PmrD is found to protect phospho-PmrA and prolong the expression of PmrA-activated genes. In contrast, Escherichia coli PmrD fails to protect phospho-PmrA. Here, we show that Klebsiella pneumoniae PmrD (KP-PmrD) can inhibit the dephosphrylation of phospho-PmrA, and the interaction between KP-PmrD and the N-terminal receiver domain of PmrA (PmrA(N)) is much stronger in the presence than in the absence of the phosphoryl analog beryllofluoride (BeF(3)(-)) (K(D) = 1.74 +/- 0.81 mu M vs. K(D) = 236 +/- 48 mu M). To better understand the molecular interactions involved, the solution structure of KP-PmrD was found to comprise six beta-strands and a flexible C-terminal alpha-helix. Amide chemical shift perturbations of KP-PmrD in complex with BeF(3)(-)-activated PmrA(N) suggested that KP-PmrD may undergo a certain conformational rearrangement on binding to activated PmrA(N). Saturation transfer experiments revealed the binding surface to be located on one face of the beta-barrel. This finding was further verified by in vivo polymyxin B susceptibility assay of the mutants of KP-PmrD. The phospho-PmrA recognition surface of KP-PmrD, which involves two KP-PmrD proteins in complex with an activated-PmrA(N) dimer, is suggested to be a contiguous patch consisting of Trp3, Trp4, Ser23, Leu26, Glu27, Met28, Thr46, Leu48, Ala49, Asp50, Ala51, Arg52,Ile65, Asn67, Ala68, Thr69, His70, Tyr71, Ser73 and Glu74. Our study furthers the understanding of how PmrD protects phopho-PmrA in the PmrAB TCS. (C) 2010 Elsevier Inc. All rights reserved.en_US
dc.language.isoen_USen_US
dc.subjectNMRen_US
dc.subjectSPRen_US
dc.subjectPmrD connector proteinen_US
dc.subjectChemical shift perturbationen_US
dc.subjectSaturation transferen_US
dc.subjectBeF(3)(-) activationen_US
dc.titleSolution structure and phospho-PmrA recognition mode of PmrD from Klebsiella pneumoniaeen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.jsb.2010.06.007en_US
dc.identifier.journalJOURNAL OF STRUCTURAL BIOLOGYen_US
dc.citation.volume172en_US
dc.citation.issue3en_US
dc.citation.spage319en_US
dc.citation.epage330en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.identifier.wosnumberWOS:000283964000015-
dc.citation.woscount4-
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