2yn0: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 2yn0 is ~~ON HOLD~~

==tau55 histidine phosphatase domain==

== 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>

== 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.

~~Authors:~~ Taylor~~, N.M.I.~~, Glatt, S., von Scheven, G., Fernandez-Tornero, C., Rybin, V., Kolb, P., Muller~~, C~~.W.

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>

~~Description~~: ~~tau55 histidine phosphatase domain~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Transcription factor tau|Transcription factor tau]]

== 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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2yn0 is ON HOLD
+==tau55 histidine phosphatase domain==
+<StructureSection load='2yn0' size='340' side='right'caption='[[2yn0]], [[Resolution|resolution]] 1.50&Aring;' 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]] 1.5&#8491;</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.
-Authors: Taylor, N.M.I., Glatt, S., von Scheven, G., Fernandez-Tornero, C., Rybin, V., Kolb, P., Muller, C.W.
+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>
-Description: tau55 histidine phosphatase domain
+From MEDLINE&reg;/PubMed&reg;, 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]]