| http://purl.uniprot.org/citations/16533062 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16533062 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16533062 | http://www.w3.org/2000/01/rdf-schema#comment | "Blue-light sensing proteins that use FAD (BLUF) are members of a blue-light receptor family that is widely distributed among microorganisms. The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain. The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity. Light-induced structural changes for the signaling state formation were studied using the light-induced Fourier transform infrared (FTIR) difference spectroscopy of both the full-length YcgF protein (YcgF-Full) and its BLUF domain (YcgF-BLUF). YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics. The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum. These bands were assigned to the light-induced structural changes of the protein. However, the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF. Furthermore, the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands. The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi051820x"xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi051820x"xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/author | "Hasegawa K."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/author | "Hasegawa K."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/author | "Masuda S."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/author | "Masuda S."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/author | "Ono T.A."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/author | "Ono T.A."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/pages | "3785-3793"xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/pages | "3785-3793"xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/title | "Light induced structural changes of a full-length protein and its BLUF domain in YcgF(Blrp), a blue-light sensing protein that uses FAD (BLUF)."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/title | "Light induced structural changes of a full-length protein and its BLUF domain in YcgF(Blrp), a blue-light sensing protein that uses FAD (BLUF)."xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/volume | "45"xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://purl.uniprot.org/core/volume | "45"xsd:string |
| http://purl.uniprot.org/citations/16533062 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16533062 |
| http://purl.uniprot.org/citations/16533062 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16533062 |
| http://purl.uniprot.org/citations/16533062 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16533062 |
| http://purl.uniprot.org/citations/16533062 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16533062 |