5c2y
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c2y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C2Y FirstGlance]. <br> | <table><tr><td colspan='2'>[[5c2y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C2Y FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5c2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c2y OCA], [https://pdbe.org/5c2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c2y RCSB], [https://www.ebi.ac.uk/pdbsum/5c2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c2y ProSAT]</span></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=5c2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c2y OCA], [https://pdbe.org/5c2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c2y RCSB], [https://www.ebi.ac.uk/pdbsum/5c2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c2y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RTR1_YEAST RTR1_YEAST] RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase that dephosphorylates 'Ser-5' of the CTD and regulates RNA polymerase II during the transition from 'Ser-5' to 'Ser-2' phosphorylation.<ref>PMID:18408053</ref> <ref>PMID:19394294</ref> | [https://www.uniprot.org/uniprot/RTR1_YEAST RTR1_YEAST] RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase that dephosphorylates 'Ser-5' of the CTD and regulates RNA polymerase II during the transition from 'Ser-5' to 'Ser-2' phosphorylation.<ref>PMID:18408053</ref> <ref>PMID:19394294</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Changes in the phosphorylation status of the carboxyl-terminal domain (CTD) of RNA polymerase II (RNAPII) correlate with the process of eukaryotic transcription. The yeast protein regulator of transcription 1 (Rtr1) and the human homolog RNAPII-associated protein 2 (RPAP2) may function as CTD phosphatases; however, crystal structures of Kluyveromyces lactis Rtr1 lack a consensus active site. We identified a phosphoryl transfer domain in Saccharomyces cerevisiae Rtr1 by obtaining and characterizing a 2.6 A resolution crystal structure. We identified a putative substrate-binding pocket in a deep groove between the zinc finger domain and a pair of helices that contained a trapped sulfate ion. Because sulfate mimics the chemistry of a phosphate group, this structural data suggested that this groove represents the phosphoryl transfer active site. Mutagenesis of the residues lining this groove disrupted catalytic activity of the enzyme assayed in vitro with a fluorescent chemical substrate, and expression of the mutated Rtr1 failed to rescue growth of yeast lacking Rtr1. Characterization of the phosphatase activity of RPAP2 and a mutant of the conserved putative catalytic site in the same chemical assay indicated a conserved reaction mechanism. Our data indicated that the structure of the phosphoryl transfer domain and reaction mechanism for the phosphoryl transfer activity of Rtr1 is distinct from those of other phosphatase families. | ||
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| - | Structure of Saccharomyces cerevisiae Rtr1 reveals an active site for an atypical phosphatase.,Irani S, Yogesha SD, Mayfield J, Zhang M, Zhang Y, Matthews WL, Nie G, Prescott NA, Zhang YJ Sci Signal. 2016 Mar 1;9(417):ra24. doi: 10.1126/scisignal.aad4805. PMID:26933063<ref>PMID:26933063</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5c2y" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of the Saccharomyces cerevisiae Rtr1 (regulator of transcription)
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