| http://purl.uniprot.org/citations/24531929 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24531929 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24531929 | http://www.w3.org/2000/01/rdf-schema#comment | "The teicoplanin-associated locus regulator (TcaR) regulates gene expression of proteins on the intercellular adhesion (ica) locus involved in staphylococci poly-N-acetylglucosamine biosynthesis. The absence of TcaR increases poly-N-acetylglucosamine production and promotes biofilm formation. Until recently, the mechanism of multiple antibiotic resistance regulator family protein members, such as TcaR, was restricted to binding double-stranded DNA. However, we recently found that TcaR strongly interacts with single-stranded DNA, which is a new role for this family of proteins. In this study, we report Staphylococcus epidermidis TcaR-single-stranded DNA complex structures. Our model suggests that TcaR and single-stranded DNA form a 61-symmetry polymer composed of TcaR dimers with single-stranded DNA that wraps outside the polymer and 12 nt per TcaR dimer. Single-stranded DNA binding to TcaR involves a large conformational change at the DNA binding lobe. Several point mutations involving the single-stranded DNA binding surface validate interactions between single-stranded DNA and TcaR. Our results extend the novel role of multiple antibiotic resistance regulator family proteins in staphylococci."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.org/dc/terms/identifier | "doi:10.1093/nar/gku128"xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.org/dc/terms/identifier | "doi:10.1093/nar/gku128"xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Ho C.H."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Ho C.H."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Wang A.H."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Wang A.H."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Maestre-Reyna M."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Maestre-Reyna M."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Chen C.K."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Chen C.K."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Chang Y.M."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Chang Y.M."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Chang-Chien M.W."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/author | "Chang-Chien M.W."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/name | "Nucleic Acids Res."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/name | "Nucleic Acids Res"xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/pages | "5314-5321"xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/pages | "5314-5321"xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/title | "TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins."xsd:string |
| http://purl.uniprot.org/citations/24531929 | http://purl.uniprot.org/core/title | "TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins."xsd:string |