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{{STRUCTURE_2yn0| PDB=2yn0 | SCENE= }}
==tau55 histidine phosphatase domain==
===tau55 histidine phosphatase domain===
<StructureSection load='2yn0' size='340' side='right' caption='[[2yn0]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
{{ABSTRACT_PUBMED_23569204}}
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2yn0]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YN0 FirstGlance]. <br>
==Function==
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yn0 RCSB], [http://www.ebi.ac.uk/pdbsum/2yn0 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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>   
[[http://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.


==About this Structure==
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>
[[2yn0]] is a 1 chain structure with sequence from [http://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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:023569204</ref><references group="xtra"/><references/>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Fernandez-Tornero, C.]]
[[Category: Fernandez-Tornero, C]]
[[Category: Gavin, A C.]]
[[Category: Gavin, A C]]
[[Category: Glatt, S.]]
[[Category: Glatt, S]]
[[Category: Grotsch, H.]]
[[Category: Grotsch, H]]
[[Category: Hennrich, M.]]
[[Category: Hennrich, M]]
[[Category: Kolb, P.]]
[[Category: Kolb, P]]
[[Category: Muller, C W.]]
[[Category: Muller, C W]]
[[Category: Rybin, V.]]
[[Category: Rybin, V]]
[[Category: Scheven, G von.]]
[[Category: Scheven, G von]]
[[Category: Taylor, N M.I.]]
[[Category: Taylor, N M.I]]
[[Category: Rna polymerase iii]]
[[Category: Rna polymerase iii]]
[[Category: Transcription]]
[[Category: Transcription]]

Revision as of 12:50, 25 December 2014

tau55 histidine phosphatase domaintau55 histidine phosphatase domain

Structural highlights

2yn0 is a 1 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, RCSB, PDBsum

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 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[2]

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

References

  1. ↑ Manaud N, Arrebola R, Buffin-Meyer B, Lefebvre O, Voss H, Riva M, Conesa C, Sentenac A. A chimeric subunit of yeast transcription factor IIIC forms a subcomplex with tau95. Mol Cell Biol. 1998 Jun;18(6):3191-200. PMID:9584160
  2. ↑ Taylor NM, Glatt S, Hennrich ML, von Scheven G, Grotsch H, Fernandez-Tornero C, Rybin V, Gavin AC, Kolb P, Muller CW. Structural and functional characterization of a phosphatase domain within yeast general transcription factor TFIIIC. J Biol Chem. 2013 Apr 8. PMID:23569204 doi:10.1074/jbc.M112.427856

2yn0, resolution 1.50Å

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