5zyp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:25, 23 May 2019) (edit) (undo)
 
Line 1: Line 1:
==Structure of the Yeast Ctr9/Paf1 complex==
==Structure of the Yeast Ctr9/Paf1 complex==
-
<StructureSection load='5zyp' size='340' side='right' caption='[[5zyp]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
+
<StructureSection load='5zyp' size='340' side='right'caption='[[5zyp]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5zyp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZYP FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5zyp]] 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=5ZYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZYP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAF1, YBR279W, YBR2016 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5zyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zyp OCA], [http://pdbe.org/5zyp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zyp RCSB], [http://www.ebi.ac.uk/pdbsum/5zyp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zyp ProSAT]</span></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=5zyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zyp OCA], [http://pdbe.org/5zyp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zyp RCSB], [http://www.ebi.ac.uk/pdbsum/5zyp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zyp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CTR9_YEAST CTR9_YEAST]] The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. In complex with PAF1, required for normal CLN1 and CLN2 G1 cyclin expression in late G1. Also has a role in chromosome segregation where it appears to be involved in microtubule placement.<ref>PMID:10219085</ref> <ref>PMID:15643076</ref> <ref>PMID:16246725</ref> <ref>PMID:8978028</ref>
[[http://www.uniprot.org/uniprot/CTR9_YEAST CTR9_YEAST]] The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. In complex with PAF1, required for normal CLN1 and CLN2 G1 cyclin expression in late G1. Also has a role in chromosome segregation where it appears to be involved in microtubule placement.<ref>PMID:10219085</ref> <ref>PMID:15643076</ref> <ref>PMID:16246725</ref> <ref>PMID:8978028</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The evolutionarily conserved multifunctional polymerase-associated factor 1 (Paf1) complex (Paf1C), which is composed of at least five subunits (Paf1, Leo1, Ctr9, Cdc73, and Rtf1), plays vital roles in gene regulation and has connections to development and human diseases. Here, we report two structures of each of the human and yeast Ctr9/Paf1 subcomplexes, which assemble into heterodimers with very similar conformations, revealing an interface between the tetratricopeptide repeat module in Ctr9 and Paf1. The structure of the Ctr9/Paf1 subcomplex may provide mechanistic explanations for disease-associated mutations in human PAF1 and CTR9. Our study reveals that the formation of the Ctr9/Paf1 heterodimer is required for the assembly of yeast Paf1C, and is essential for yeast viability. In addition, disruption of the interaction between Paf1 and Ctr9 greatly affects the level of histone H3 methylation in vivo. Collectively, our results shed light on Paf1C assembly and functional regulation.
 +
 +
Paf1 and Ctr9 subcomplex formation is essential for Paf1 complex assembly and functional regulation.,Xie Y, Zheng M, Chu X, Chen Y, Xu H, Wang J, Zhou H, Long J Nat Commun. 2018 Sep 18;9(1):3795. doi: 10.1038/s41467-018-06237-7. PMID:30228257<ref>PMID:30228257</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5zyp" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Baker's yeast]]
 +
[[Category: Large Structures]]
[[Category: Long, J]]
[[Category: Long, J]]
[[Category: Xie, Y]]
[[Category: Xie, Y]]

Current revision

Structure of the Yeast Ctr9/Paf1 complex

PDB ID 5zyp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5zyp"
Personal tools