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Structure-Function Analysis of Arabidopsis thaliana Histidine Kinase AHK5 Bound to Its Cognate Phosphotransfer Protein AHP1

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Molecular Plant 2013年第3期6卷 959-970页

作者： Johannes Bauer Kerstin Reiss Manikandan Veerabagu Michael Heunemann Klaus Harter Thilo Stehle Interfaculty Institute of Biochemistry University of Tubingen D-72076 Tubingen Germany Center for Plant Molecular Biology University of TObingen D-72076 T0bingen Germany Department of Pediatrics Vanderbilt University School of Medicine Nashville TN 37232 USA

The multi-step phosphorelay （MSP） system.defines a key signal transduction pathway in plants and many eukaryotes. In this system. external stimuli first lead to the activation of a histidine kinase, followed by transfer of a phosphoryl group from the receiver domain of the kinase （HKRD） to downstream, cytosolic phosphotransfer proteins （HPs）. In order to establish the determinants of specificity for this signaling relay system. we have solved the first crystal structure of a plant HKRD, AHK5RD, in complex with one of its cognate HPs, AHP1. AHP1 binds AHK5RD via a prominent hydrogen bond docking ridge and a hydrophobic patch. These features are conserved among all AHP proteins, but differ significantly from other structurally characterized prokaryotic and eukaryotic HPs. Surface plasmon resonance experiments show that AHK5RD binds to AHP1-3 with similar, micromolar affinity, consistent with the transient nature of this signaling complex. Our correlation of structural and functional data provide the first insight, at the atomic level as well as with quantitative affinity data, into the molecular recognition events governing the MSP in plants.

关键词： multi-step phosphorelay phosphotransfer protein plant signaling sensor histidine kinase two-component system.

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Molecular Cloning of PhoR Sensor Domain from Mycobacterium tuberculosis for Structure-Based Discovery of Novel Anti-Tubercular

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Journal of Life Sciences 2012年第3期6卷 268-275页

作者： Aldina S. Suwanto Ihsanawati Emawati Arifin Giri-Rachman School of Life Sciences and Technology Bandung Institute of Technology Bandung 40132 Indonesia Biochemistry Research Group Faculty of Mathematics and Natural Sciences Bandung Institute of Technology Bandung40132 Indonesia

The emergence of multidrug-resistant strains （MDR-TB） and extensively drug-resistant strains （XDR-TB） has fuelled the quest for novel drugs and drug targets for its successful treatment. One of the potential candidates as novel TB drug target is the PhoR sensor domain, an extracellular domain of PhoR histidine kinase. PhoR sensor domain is part of the two-component system.PhoR-PhoP that senses environmental stimuli and relays the signal to control the expression of 78 virulent associated genes in Mycobacterium tuberculosis. 3D structure of the PhoR sensor domain will facilitate the structure based drug discovery of novel anti- tubercular. In this study, we successfully predicted and isolated the gene encoding PhoR sensor domain from Mycobacterium tuberculosis H37Rv, cloned it in pGEM-T vector and subcloned it in pRSET emGFP expression vector. PhoR sensor domain was successfully cloned and would be used for further expression, purification and crystallization studies.

关键词： Sensor domain PhoR tuberculosis two-component system.

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