2yn0: Difference between revisions
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==tau55 histidine phosphatase domain== | |||
<StructureSection load='2yn0' size='340' side='right'caption='[[2yn0]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2yn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2YN0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yn0 OCA], [https://pdbe.org/2yn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yn0 RCSB], [https://www.ebi.ac.uk/pdbsum/2yn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yn0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TFC7_YEAST 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.<ref>PMID:9584160</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Saccharomyces 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<ref>PMID:23569204</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2yn0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transcription factor tau|Transcription factor tau]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Fernandez-Tornero C]] | |||
[[Category: Gavin AC]] | |||
[[Category: Glatt S]] | |||
[[Category: Grotsch H]] | |||
[[Category: Hennrich M]] | |||
[[Category: Kolb P]] | |||
[[Category: Muller CW]] | |||
[[Category: Rybin V]] | |||
[[Category: Taylor NMI]] | |||
[[Category: Von Scheven G]] | |||
Latest revision as of 16:37, 30 August 2023
tau55 histidine phosphatase domaintau55 histidine phosphatase domain
Structural highlights
FunctionTFC7_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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