| http://purl.uniprot.org/citations/24055315 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24055315 | http://www.w3.org/2000/01/rdf-schema#comment | "CarD from Mycobacterium tuberculosis (Mtb) is an essential protein shown to be involved in stringent response through downregulation of rRNA and ribosomal protein genes. CarD interacts with the β-subunit of RNAP and this interaction is vital for Mtb's survival during the persistent infection state. We have determined the crystal structure of CarD in complex with the RNAP β-subunit β1 and β2 domains at 2.1 Å resolution. The structure reveals the molecular basis of CarD/RNAP interaction, providing a basis to further our understanding of RNAP regulation by CarD. The structural fold of the CarD N-terminal domain is conserved in RNAP interacting proteins such as TRCF-RID and CdnL, and displays similar interactions to the predicted homology model based on the TRCF/RNAP β1 structure. Interestingly, the structure of the C-terminal domain, which is required for complete CarD function in vivo, represents a distinct DNA-binding fold."xsd:string |
| http://purl.uniprot.org/citations/24055315 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.str.2013.08.014"xsd:string |
| http://purl.uniprot.org/citations/24055315 | http://purl.uniprot.org/core/author | "Sacchettini J.C."xsd:string |
| http://purl.uniprot.org/citations/24055315 | http://purl.uniprot.org/core/author | "Gulten G."xsd:string |
| http://purl.uniprot.org/citations/24055315 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24055315 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
| http://purl.uniprot.org/citations/24055315 | http://purl.uniprot.org/core/pages | "1859-1869"xsd:string |
| http://purl.uniprot.org/citations/24055315 | http://purl.uniprot.org/core/title | "Structure of the Mtb CarD/RNAP beta-lobes complex reveals the molecular basis of interaction and presents a distinct DNA-binding domain for Mtb CarD."xsd:string |
| http://purl.uniprot.org/citations/24055315 | http://purl.uniprot.org/core/volume | "21"xsd:string |
| http://purl.uniprot.org/citations/24055315 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24055315 |
| http://purl.uniprot.org/citations/24055315 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24055315 |
| http://purl.uniprot.org/uniprot/#_P9WGY9-mappedCitation-24055315 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24055315 |
| http://purl.uniprot.org/uniprot/#_P9WJG3-mappedCitation-24055315 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24055315 |
| http://purl.uniprot.org/uniprot/P9WJG3 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/24055315 |
| http://purl.uniprot.org/uniprot/P9WGY9 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/24055315 |