Insights into the structure and function of the histidine kinase ComP from Bacillus amyloliquefaciens based on molecular modeling
The ComPA two-component signal transduction system (TCS) is essential in Bacillus spp. However, the molecular mechanism of the histidine kinase ComP remains unclear. Here, we predicted the structure of ComP from Bacillus amyloliquefaciens Q-426 (BaComP) using an artificial intelligence approach, ana...
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| Veröffentlicht in: | Bioscience reports 2022-10, Vol.42 (10), p.1 |
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| creator | Wang, Lulu Fan, Ruochen Li, Zhuting Wang, Lina Bai, Xue Bu, Tingting Dong, Yuesheng Xu, Yongbin Quan, Chunshan |
| description | The ComPA two-component signal transduction system (TCS) is essential in Bacillus spp. However, the molecular mechanism of the histidine kinase ComP remains unclear. Here, we predicted the structure of ComP from Bacillus amyloliquefaciens Q-426 (BaComP) using an artificial intelligence approach, analyzed the structural characteristics based on the molecular docking results and compared homologous proteins, and then investigated the biochemical properties of BaComP. We obtained a truncated ComPS protein with high purity and correct folding in solution based on the predicted structures. The expression and purification of BaComP proteins suggested that the subdomains in the cytoplasmic region influenced the expression and stability of the recombinant proteins. ComPS is a bifunctional enzyme that exhibits the activity of both histidine kinase and phosphotransferase. We found that His571 played an obligatory role in the autophosphorylation of BaComP based on the analysis of the structures and mutagenesis studies. The molecular docking results suggested that the HATPase_c domain contained an ATP-binding pocket, and the ATP molecule was coordinated by eight conserved residues from the N, G1, and G2 boxes. Our study provides novel insight into the histidine kinase BaComP and its homologous proteins. |
| doi_str_mv | 10.1042/BSR20220352 |
| format | Article |
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Here, we predicted the structure of ComP from Bacillus amyloliquefaciens Q-426 (BaComP) using an artificial intelligence approach, analyzed the structural characteristics based on the molecular docking results and compared homologous proteins, and then investigated the biochemical properties of BaComP. We obtained a truncated ComPS protein with high purity and correct folding in solution based on the predicted structures. The expression and purification of BaComP proteins suggested that the subdomains in the cytoplasmic region influenced the expression and stability of the recombinant proteins. ComPS is a bifunctional enzyme that exhibits the activity of both histidine kinase and phosphotransferase. We found that His571 played an obligatory role in the autophosphorylation of BaComP based on the analysis of the structures and mutagenesis studies. The molecular docking results suggested that the HATPase_c domain contained an ATP-binding pocket, and the ATP molecule was coordinated by eight conserved residues from the N, G1, and G2 boxes. Our study provides novel insight into the histidine kinase BaComP and its homologous proteins.</description><identifier>ISSN: 0144-8463</identifier><identifier>ISSN: 1573-4935</identifier><identifier>EISSN: 1573-4935</identifier><identifier>DOI: 10.1042/BSR20220352</identifier><identifier>PMID: 36052710</identifier><language>eng</language><publisher>England: Portland Press Ltd The Biochemical Society</publisher><subject>Adenosine Triphosphate - metabolism ; Amino acids ; Artificial Intelligence ; ATP ; Bacillus amyloliquefaciens ; Bacillus amyloliquefaciens - genetics ; Bacillus amyloliquefaciens - metabolism ; Bacterial Proteins - metabolism ; Glycerol ; Histidine ; Histidine kinase ; Histidine Kinase - genetics ; Histidine Kinase - metabolism ; Homology ; Kinases ; Methods ; Molecular docking ; Molecular Docking Simulation ; Molecular modelling ; Mutagenesis ; Phosphorylation ; Phosphotransferase ; Plasmids ; Protein folding ; Protein Kinases - metabolism ; Protein purification ; Proteins ; Signal transduction ; Spectrum analysis ; Structure-function relationships</subject><ispartof>Bioscience reports, 2022-10, Vol.42 (10), p.1</ispartof><rights>2022 The Author(s).</rights><rights>2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). 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Here, we predicted the structure of ComP from Bacillus amyloliquefaciens Q-426 (BaComP) using an artificial intelligence approach, analyzed the structural characteristics based on the molecular docking results and compared homologous proteins, and then investigated the biochemical properties of BaComP. We obtained a truncated ComPS protein with high purity and correct folding in solution based on the predicted structures. The expression and purification of BaComP proteins suggested that the subdomains in the cytoplasmic region influenced the expression and stability of the recombinant proteins. ComPS is a bifunctional enzyme that exhibits the activity of both histidine kinase and phosphotransferase. We found that His571 played an obligatory role in the autophosphorylation of BaComP based on the analysis of the structures and mutagenesis studies. The molecular docking results suggested that the HATPase_c domain contained an ATP-binding pocket, and the ATP molecule was coordinated by eight conserved residues from the N, G1, and G2 boxes. Our study provides novel insight into the histidine kinase BaComP and its homologous proteins.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino acids</subject><subject>Artificial Intelligence</subject><subject>ATP</subject><subject>Bacillus amyloliquefaciens</subject><subject>Bacillus amyloliquefaciens - genetics</subject><subject>Bacillus amyloliquefaciens - metabolism</subject><subject>Bacterial Proteins - metabolism</subject><subject>Glycerol</subject><subject>Histidine</subject><subject>Histidine kinase</subject><subject>Histidine Kinase - genetics</subject><subject>Histidine Kinase - metabolism</subject><subject>Homology</subject><subject>Kinases</subject><subject>Methods</subject><subject>Molecular docking</subject><subject>Molecular Docking Simulation</subject><subject>Molecular modelling</subject><subject>Mutagenesis</subject><subject>Phosphorylation</subject><subject>Phosphotransferase</subject><subject>Plasmids</subject><subject>Protein folding</subject><subject>Protein Kinases - 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Academic</collection><jtitle>Bioscience reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Lulu</au><au>Fan, Ruochen</au><au>Li, Zhuting</au><au>Wang, Lina</au><au>Bai, Xue</au><au>Bu, Tingting</au><au>Dong, Yuesheng</au><au>Xu, Yongbin</au><au>Quan, Chunshan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insights into the structure and function of the histidine kinase ComP from Bacillus amyloliquefaciens based on molecular modeling</atitle><jtitle>Bioscience reports</jtitle><addtitle>Biosci Rep</addtitle><date>2022-10-28</date><risdate>2022</risdate><volume>42</volume><issue>10</issue><spage>1</spage><pages>1-</pages><issn>0144-8463</issn><issn>1573-4935</issn><eissn>1573-4935</eissn><abstract>The ComPA two-component signal transduction system (TCS) is essential in Bacillus spp. However, the molecular mechanism of the histidine kinase ComP remains unclear. Here, we predicted the structure of ComP from Bacillus amyloliquefaciens Q-426 (BaComP) using an artificial intelligence approach, analyzed the structural characteristics based on the molecular docking results and compared homologous proteins, and then investigated the biochemical properties of BaComP. We obtained a truncated ComPS protein with high purity and correct folding in solution based on the predicted structures. The expression and purification of BaComP proteins suggested that the subdomains in the cytoplasmic region influenced the expression and stability of the recombinant proteins. ComPS is a bifunctional enzyme that exhibits the activity of both histidine kinase and phosphotransferase. We found that His571 played an obligatory role in the autophosphorylation of BaComP based on the analysis of the structures and mutagenesis studies. The molecular docking results suggested that the HATPase_c domain contained an ATP-binding pocket, and the ATP molecule was coordinated by eight conserved residues from the N, G1, and G2 boxes. Our study provides novel insight into the histidine kinase BaComP and its homologous proteins.</abstract><cop>England</cop><pub>Portland Press Ltd The Biochemical Society</pub><pmid>36052710</pmid><doi>10.1042/BSR20220352</doi><orcidid>https://orcid.org/0000-0002-1537-3964</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Triphosphate - metabolism Amino acids Artificial Intelligence ATP Bacillus amyloliquefaciens Bacillus amyloliquefaciens - genetics Bacillus amyloliquefaciens - metabolism Bacterial Proteins - metabolism Glycerol Histidine Histidine kinase Histidine Kinase - genetics Histidine Kinase - metabolism Homology Kinases Methods Molecular docking Molecular Docking Simulation Molecular modelling Mutagenesis Phosphorylation Phosphotransferase Plasmids Protein folding Protein Kinases - metabolism Protein purification Proteins Signal transduction Spectrum analysis Structure-function relationships |
| title | Insights into the structure and function of the histidine kinase ComP from Bacillus amyloliquefaciens based on molecular modeling |
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