3v46: Difference between revisions

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==Crystal Structure of Yeast Cdc73 C-Terminal Domain==
==Crystal Structure of Yeast Cdc73 C-Terminal Domain==
<StructureSection load='3v46' size='340' side='right' caption='[[3v46]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
<StructureSection load='3v46' size='340' side='right'caption='[[3v46]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3v46]] 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=3V46 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V46 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3v46]] 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=3V46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V46 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC73, YLR418C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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]] 1.549&#8491;</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=3v46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v46 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v46 RCSB], [http://www.ebi.ac.uk/pdbsum/3v46 PDBsum]</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=3v46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v46 OCA], [https://pdbe.org/3v46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v46 RCSB], [https://www.ebi.ac.uk/pdbsum/3v46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v46 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/CDC73_YEAST CDC73_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.<ref>PMID:9032243</ref> <ref>PMID:15643076</ref> <ref>PMID:16246725</ref>  
The conserved Paf1 complex localizes to the coding regions of genes and facilitates multiple processes during transcription elongation, including the regulation of histone modifications. However, the mechanisms that govern Paf1 complex recruitment to active genes are undefined. Here we describe a previously unrecognized domain within the Cdc73 subunit of the Paf1 complex, the Cdc73 C-domain, and demonstrate its importance for Paf1 complex occupancy on transcribed chromatin. Deletion of the C-domain causes phenotypes associated with elongation defects without an apparent loss of complex integrity. Simultaneous mutation of the C-domain and another subunit of the Paf1 complex, Rtf1, causes enhanced mutant phenotypes and loss of histone H3 lysine 36 trimethylation. The crystal structure of the C-domain reveals unexpected similarity to the Ras family of small GTPases. Instead of a deep nucleotide-binding pocket, the C-domain contains a large but comparatively flat surface of highly conserved residues, devoid of ligand. Deletion of the C-domain results in reduced chromatin association for multiple Paf1 complex subunits. We conclude that the Cdc73 C-domain probably constitutes a protein interaction surface that functions with Rtf1 in coupling the Paf1 complex to the RNA polymerase II elongation machinery.
 
Cdc73 subunit of Paf1 complex contains C-terminal Ras-like domain that promotes association of Paf1 complex with chromatin.,Amrich CG, Davis CP, Rogal WP, Shirra MK, Heroux A, Gardner RG, Arndt KM, VanDemark AP J Biol Chem. 2012 Mar 30;287(14):10863-75. Epub 2012 Feb 8. PMID:22318720<ref>PMID:22318720</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Large Structures]]
[[Category: Amrich, C G]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: VanDemark, A P]]
[[Category: Amrich CG]]
[[Category: Non-gtp binding]]
[[Category: VanDemark AP]]
[[Category: Protein interaction surface]]
[[Category: Ras-like fold]]
[[Category: Transcription]]
[[Category: Transcription elongation factor]]

Latest revision as of 13:31, 1 March 2024

Crystal Structure of Yeast Cdc73 C-Terminal DomainCrystal Structure of Yeast Cdc73 C-Terminal Domain

Structural highlights

3v46 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.
Method:X-ray diffraction, Resolution 1.549Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CDC73_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.[1] [2] [3]

References

  1. ↑ Shi X, Chang M, Wolf AJ, Chang CH, Frazer-Abel AA, Wade PA, Burton ZF, Jaehning JA. Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex distinct from the Srbp-containing holoenzyme. Mol Cell Biol. 1997 Mar;17(3):1160-9. PMID:9032243
  2. ↑ Porter SE, Penheiter KL, Jaehning JA. Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization. Eukaryot Cell. 2005 Jan;4(1):209-20. PMID:15643076 doi:http://dx.doi.org/10.1128/EC.4.1.209-220.2005
  3. ↑ Sheldon KE, Mauger DM, Arndt KM. A Requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation. Mol Cell. 2005 Oct 28;20(2):225-36. PMID:16246725 doi:S1097-2765(05)01568-6

3v46, resolution 1.55Å

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