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1e0n

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Revision as of 10:37, 14 December 2022

YJQ8WW domain from Saccharomyces cerevisae

Structural highlights

1e0n is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SET2_YEAST Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands. The structural roles of conserved residues have been studied using site-directed mutagenesis of both wild type domains. Crucial interactions responsible for the stability of the WW structure have been identified. Based on a network of highly conserved long range interactions across the beta-sheet structure that supports the WW fold and on a systematic analysis of conserved residues in the WW family, we have designed a folded prototype WW sequence.

Structural analysis of WW domains and design of a WW prototype.,Macias MJ, Gervais V, Civera C, Oschkinat H Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733^[8]

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

References

↑ Strahl BD, Grant PA, Briggs SD, Sun ZW, Bone JR, Caldwell JA, Mollah S, Cook RG, Shabanowitz J, Hunt DF, Allis CD. Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression. Mol Cell Biol. 2002 Mar;22(5):1298-306. PMID:11839797
↑ Xiao T, Hall H, Kizer KO, Shibata Y, Hall MC, Borchers CH, Strahl BD. Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast. Genes Dev. 2003 Mar 1;17(5):654-63. PMID:12629047 doi:http://dx.doi.org/10.1101/gad.1055503
↑ Schaft D, Roguev A, Kotovic KM, Shevchenko A, Sarov M, Shevchenko A, Neugebauer KM, Stewart AF. The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation. Nucleic Acids Res. 2003 May 15;31(10):2475-82. doi: 10.1093/nar/gkg372. PMID:12736296 doi:http://dx.doi.org/10.1093/nar/gkg372
↑ Krogan NJ, Kim M, Tong A, Golshani A, Cagney G, Canadien V, Richards DP, Beattie BK, Emili A, Boone C, Shilatifard A, Buratowski S, Greenblatt J. Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II. Mol Cell Biol. 2003 Jun;23(12):4207-18. doi: 10.1128/MCB.23.12.4207-4218.2003. PMID:12773564 doi:http://dx.doi.org/10.1128/MCB.23.12.4207-4218.2003
↑ Landry J, Sutton A, Hesman T, Min J, Xu RM, Johnston M, Sternglanz R. Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae. Mol Cell Biol. 2003 Sep;23(17):5972-8. doi: 10.1128/MCB.23.17.5972-5978.2003. PMID:12917322 doi:http://dx.doi.org/10.1128/MCB.23.17.5972-5978.2003
↑ Kizer KO, Phatnani HP, Shibata Y, Hall H, Greenleaf AL, Strahl BD. A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. Mol Cell Biol. 2005 Apr;25(8):3305-16. PMID:15798214 doi:http://dx.doi.org/25/8/3305
↑ Rao B, Shibata Y, Strahl BD, Lieb JD. Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide. Mol Cell Biol. 2005 Nov;25(21):9447-59. PMID:16227595 doi:http://dx.doi.org/25/21/9447
↑ Macias MJ, Gervais V, Civera C, Oschkinat H. Structural analysis of WW domains and design of a WW prototype. Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733 doi:10.1038/75144

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e0n"

@@ Line 1: / Line 1: @@
 ==YJQ8WW domain from Saccharomyces cerevisae==
-<StructureSection load='1e0n' size='340' side='right'caption='[[1e0n]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1e0n' size='340' side='right'caption='[[1e0n]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1e0n]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1e0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0N FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e0m|1e0m]], [[1e0l|1e0l]]</div></td></tr>
+</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=1e0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0n OCA], [https://pdbe.org/1e0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0n RCSB], [https://www.ebi.ac.uk/pdbsum/1e0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0n 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=1e0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0n OCA], [https://pdbe.org/1e0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0n RCSB], [https://www.ebi.ac.uk/pdbsum/1e0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0n ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SET2_YEAST SET2_YEAST] Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent.<ref>PMID:11839797</ref> <ref>PMID:12629047</ref> <ref>PMID:12736296</ref> <ref>PMID:12773564</ref> <ref>PMID:12917322</ref> <ref>PMID:15798214</ref> <ref>PMID:16227595</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Civera, C]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Gervais, V]]
+[[Category: Civera C]]
-[[Category: Macias, M J]]
+[[Category: Gervais V]]
-[[Category: Oschkinat, H]]
+[[Category: Macias MJ]]
-[[Category: Saccharomyces cerevisae]]
+[[Category: Oschkinat H]]
-[[Category: Ww domain]]
-[[Category: Yjq8 protein]]
-[[Category: Yjq8ww domain]]

1e0n

From Proteopedia

Revision as of 10:37, 14 December 2022

YJQ8WW domain from Saccharomyces cerevisae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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