2yn0: Difference between revisions
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==tau55 histidine phosphatase domain== | ==tau55 histidine phosphatase domain== | ||
<StructureSection load='2yn0' size='340' side='right' caption='[[2yn0]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='2yn0' size='340' side='right'caption='[[2yn0]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YN0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2yn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YN0 FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2yn0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2yn0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Transcription factor tau|Transcription factor tau]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Baker's yeast]] | [[Category: Baker's yeast]] | ||
[[Category: Large Structures]] | |||
[[Category: Fernandez-Tornero, C]] | [[Category: Fernandez-Tornero, C]] | ||
[[Category: Gavin, A C]] | [[Category: Gavin, A C]] | ||
Revision as of 10:39, 3 April 2019
tau55 histidine phosphatase domaintau55 histidine phosphatase domain
Structural highlights
Function[TFC7_YEAST] TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes.[1] Publication Abstract from PubMedSaccharomyces cerevisiae tau55, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an N-terminal histidine phosphatase domain (tau55-HPD) whose catalytic activity and cellular function is poorly understood. We solved the crystal structures of tau55-HPD and its closely related paralogue Huf and used in silico docking methods to identify phospho-serine and phospho-tyrosine containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. A comparative phospho-proteomic study identified additional phosphopeptides as possible targets, which show the involvement of these two phosphatases in the regulation of a variety of cellular functions. Our results identify tau55-HPD and Huf as bona fide protein phosphatases, characterize their substrate specificities and provide a small set of regulated phosphosite targets in vivo. Structural and functional characterization of a phosphatase domain within yeast general transcription factor TFIIIC.,Taylor NM, Glatt S, Hennrich ML, von Scheven G, Grotsch H, Fernandez-Tornero C, Rybin V, Gavin AC, Kolb P, Muller CW J Biol Chem. 2013 Apr 8. PMID:23569204[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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