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http://purl.uniprot.org/citations/19026779http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19026779http://www.w3.org/2000/01/rdf-schema#comment"Kinases and phosphatases regulate mRNA synthesis and processing by phosphorylating and dephosphorylating the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. Fcp1 is an essential CTD phosphatase that preferentially hydrolyzes Ser2-PO(4) of the tandem YSPTSPS CTD heptad array. Fcp1 crystal structures were captured at two stages of the reaction pathway: a Mg-BeF(3) complex that mimics the aspartylphosphate intermediate and a Mg-AlF(4)(-) complex that mimics the transition state of the hydrolysis step. Fcp1 is a Y-shaped protein composed of an acylphosphatase domain located at the base of a deep canyon formed by flanking modules that are missing from the small CTD phosphatase (SCP) clade: an Fcp1-specific helical domain and a C-terminal BRCA1 C-terminal (BRCT) domain. The structure and mutational analysis reveals that Fcp1 and Scp1 (a Ser5-selective phosphatase) adopt different CTD-binding modes; we surmise the CTD threads through the Fcp1 canyon to access the active site."xsd:string
http://purl.uniprot.org/citations/19026779http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2008.09.021"xsd:string
http://purl.uniprot.org/citations/19026779http://purl.uniprot.org/core/author"Ghosh A."xsd:string
http://purl.uniprot.org/citations/19026779http://purl.uniprot.org/core/author"Lima C.D."xsd:string
http://purl.uniprot.org/citations/19026779http://purl.uniprot.org/core/author"Shuman S."xsd:string
http://purl.uniprot.org/citations/19026779http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19026779http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/19026779http://purl.uniprot.org/core/pages"478-490"xsd:string
http://purl.uniprot.org/citations/19026779http://purl.uniprot.org/core/title"The structure of Fcp1, an essential RNA polymerase II CTD phosphatase."xsd:string
http://purl.uniprot.org/citations/19026779http://purl.uniprot.org/core/volume"32"xsd:string
http://purl.uniprot.org/citations/19026779http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19026779
http://purl.uniprot.org/citations/19026779http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19026779
http://purl.uniprot.org/uniprot/Q9P376#attribution-DC20837F72CED1FEAF613F84D358ACD1http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/19026779
http://purl.uniprot.org/uniprot/#_A0A6A5PTT8-mappedCitation-19026779http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19026779
http://purl.uniprot.org/uniprot/#_Q03254-mappedCitation-19026779http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19026779
http://purl.uniprot.org/uniprot/#_Q9P376-mappedCitation-19026779http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19026779
http://purl.uniprot.org/uniprot/A0A6A5PTT8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19026779
http://purl.uniprot.org/uniprot/Q03254http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19026779
http://purl.uniprot.org/uniprot/Q9P376http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19026779