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Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain
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 do...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Korean Society for Molecular and Cellular Biology
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8019601/ https://www.ncbi.nlm.nih.gov/pubmed/33795535 http://dx.doi.org/10.14348/molcells.2021.2235 |
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author | Park, Sang-Sang Lee, Sangho Rhee, Dong-Kwon |
author_facet | Park, Sang-Sang Lee, Sangho Rhee, Dong-Kwon |
author_sort | Park, Sang-Sang |
collection | PubMed |
description | 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 (Å) resolution and belonged to space group P212121. The crystal unit-cell parameters were a = 25.71 (Å), b = 52.97 (Å), and c = 60.61 (Å). 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. |
format | Online Article Text |
id | pubmed-8019601 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Korean Society for Molecular and Cellular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-80196012021-04-13 Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain Park, Sang-Sang Lee, Sangho Rhee, Dong-Kwon Mol Cells Research Article 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 (Å) resolution and belonged to space group P212121. The crystal unit-cell parameters were a = 25.71 (Å), b = 52.97 (Å), and c = 60.61 (Å). 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. Korean Society for Molecular and Cellular Biology 2021-03-31 2021-03-31 /pmc/articles/PMC8019601/ /pubmed/33795535 http://dx.doi.org/10.14348/molcells.2021.2235 Text en © The Korean Society for Molecular and Cellular Biology. All rights reserved. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ |
spellingShingle | Research Article Park, Sang-Sang Lee, Sangho Rhee, Dong-Kwon Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain |
title | Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain |
title_full | Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain |
title_fullStr | Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain |
title_full_unstemmed | Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain |
title_short | Crystal Structure of the Pneumococcal Vancomycin-Resistance Response Regulator DNA-Binding Domain |
title_sort | crystal structure of the pneumococcal vancomycin-resistance response regulator dna-binding domain |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8019601/ https://www.ncbi.nlm.nih.gov/pubmed/33795535 http://dx.doi.org/10.14348/molcells.2021.2235 |
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