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http://purl.uniprot.org/citations/30521812http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30521812http://www.w3.org/2000/01/rdf-schema#comment"The β-barrel assembly machinery (BAM) complex mediates the assembly of β-barrel membrane proteins in the outer membrane. BepA, formerly known as YfgC, interacts with the BAM complex and functions as a protease/chaperone for the enhancement of the assembly and/or degradation of β-barrel membrane proteins. To elucidate the molecular mechanism underlying the dual functions of BepA, its full-length three-dimensional structure is needed. Here, we report the crystal structure of full-length BepA at 2.6-Å resolution. BepA possesses an N-terminal protease domain and a C-terminal tetratricopeptide repeat domain, which interact with each other. Domain cross-linking by structure-guided introduction of disulfide bonds did not affect the activities of BepA in vivo, suggesting that the function of this protein does not involve domain rearrangement. The full-length BepA structure is compatible with the previously proposed docking model of BAM complex and tetratricopeptide repeat domain of BepA."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2018.11.024"xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Hayashi Y."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Nakayama S."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Tanaka Y."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Kamikubo H."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Tsukazaki T."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Akiyama Y."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Daimon Y."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Iwaki S."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Narita S.I."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/author"Shahrizal M."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/pages"625-635"xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/title"Structural Basis for the Function of the beta-Barrel Assembly-Enhancing Protease BepA."xsd:string
http://purl.uniprot.org/citations/30521812http://purl.uniprot.org/core/volume"431"xsd:string
http://purl.uniprot.org/citations/30521812http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30521812
http://purl.uniprot.org/citations/30521812http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30521812
http://purl.uniprot.org/uniprot/P66948#attribution-8F22CF057C210DF2E783DF31A6C75DB8http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/30521812
http://purl.uniprot.org/uniprot/#_P66948-mappedCitation-30521812http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30521812
http://purl.uniprot.org/uniprot/P66948http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30521812