4dm4

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dm4]] is a 2 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=4DM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dm4]] is a 2 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=4DM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM4 FirstGlance]. <br>
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</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=4dm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm4 OCA], [https://pdbe.org/4dm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm4 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm4 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm4 OCA], [https://pdbe.org/4dm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm4 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm4 ProSAT]</span></td></tr>
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</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The yeast Paf1 complex (Paf1C), which is composed of the proteins Paf1, Cdc73, Ctr9, Leo1 and Rtf1, accompanies RNA polymerase II from the promoter to the 3'-end formation site of mRNA- and snoRNA-encoding genes. As one of the first identified subunits of Paf1C, yeast Cdc73 (yCdc73) takes part in many transcription-related processes, including binding to RNA polymerase II, recruitment and activation of histone-modification factors and communication with other transcriptional activators. The human homologue of yCdc73, parafibromin, has been identified as a tumour suppressor linked to breast, renal and gastric cancers. However, the functional mechanism of yCdc73 has until recently been unclear. Here, a 2.2 A resolution crystal structure of the highly conserved C-terminal region of yCdc73 is reported. It revealed that yCdc73 appears to have a GTPase-like fold. However, no GTPase activity was observed. The crystal structure of yCdc73 will shed new light on the modes of function of Cdc73 and Paf1C.
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Crystallographic analysis of the conserved C-terminal domain of transcription factor Cdc73 from Saccharomyces cerevisiae reveals a GTPase-like fold.,Chen H, Shi N, Gao Y, Li X, Teng M, Niu L Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):953-9. Epub 2012 Jul 7. PMID:22868760<ref>PMID:22868760</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4dm4" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>

Current revision

The conserved domain of yeast Cdc73

PDB ID 4dm4

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