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KMID : 0578320210440030179
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Molecules and Cells
2021 Volume.44 No. 3 p.179 ~ p.185
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Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain
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Park Sang-Sang
Lee Sang-Ho
Rhee Dong-Kwon
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Abstract
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Vancomycin response regulator (VncR) is a pneumococcal response regulator of the VncRS two-component signal transduction system (TCS) of Streptococcus pneumoniae. VncRS regulates bacterial autolysis and vancomycin resistance. VncR contains two different functional domains, the N-terminal receiver domain and C-terminal effector domain. Here, we investigated VncR C-terminal DNA binding domain (VncRc) structure using a crystallization approach. Crystallization was performed using the micro-batch method. The crystals diffracted to a 1.964 A resolution and belonged to space group P212121. The crystal unit-cell parameters were a = 25.71 A, b = 52.97 A, and c = 60.61 A. The structure of VncRc had a helix-turn-helix motif highly similar to the response regulator PhoB of Escherichia coli. In isothermal titration calorimetry and size exclusion chromatography results, VncR formed a complex with VncS, a sensor histidine kinase of pneumococcal TCS. Determination of VncR structure will provide insight into the mechanism by how VncR binds to target genes.
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KEYWORD
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crystal structure, response regulator, Streptococcus pneumoniae, VncR
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