2j8a: Difference between revisions

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 <StructureSection load='2j8a' size='340' side='right'caption='[[2j8a]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2j8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2j8a]] is a 1 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=2J8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8A FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></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]] 3&#8491;</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=2j8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8a OCA], [https://pdbe.org/2j8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8a RCSB], [https://www.ebi.ac.uk/pdbsum/2j8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8a ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SET1_YEAST SET1_YEAST] Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11751634</ref> <ref>PMID:11752412</ref> <ref>PMID:11805083</ref> <ref>PMID:11818070</ref> <ref>PMID:12060701</ref> <ref>PMID:12353038</ref> <ref>PMID:12845608</ref> <ref>PMID:14636589</ref> <ref>PMID:15949446</ref> <ref>PMID:9398665</ref> <ref>PMID:9988274</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j8a ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, in addition to its catalytic SET domain, a conserved RNA recognition motif (RRM1). We present here the crystal structure and the secondary structure assignment in solution of the Set1 RRM1. Although RRM1 has the expected betaalphabetabetaalphabeta RRM-fold, it lacks the typical RNA-binding features of these modules. RRM1 is not able to bind RNA by itself in vitro, but a construct combining RRM1 with a newly identified downstream RRM2 specifically binds RNA. In vivo, H3K4 methylation is not affected by a point mutation in RRM2 that preserves Set1 stability but affects RNA binding in vitro. In contrast mutating RRM1 destabilizes Set1 and leads to an increase of dimethylation of H3K4 at the 5'-coding region of active genes at the expense of trimethylation, whereas both, dimethylation decreases at the 3'-coding region. Taken together, our results suggest that Set1 RRMs bind RNA, but Set1 RNA-binding activity is not linked to H3K4 methylation.
-Structural characterization of Set1 RNA recognition motifs and their role in histone H3 lysine 4 methylation.,Tresaugues L, Dehe PM, Guerois R, Rodriguez-Gil A, Varlet I, Salah P, Pamblanco M, Luciano P, Quevillon-Cheruel S, Sollier J, Leulliot N, Couprie J, Tordera V, Zinn-Justin S, Chavez S, van Tilbeurgh H, Geli V J Mol Biol. 2006 Jun 23;359(5):1170-81. Epub 2006 May 9. PMID:16787775<ref>PMID:16787775</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2j8a" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
-[[Category: Histone-lysine N-methyltransferase]]
 [[Category: Large Structures]]
-[[Category: Chavez, S]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Couprie, J]]
+[[Category: Chavez S]]
-[[Category: Dehe, P M]]
+[[Category: Couprie J]]
-[[Category: Geli, V]]
+[[Category: Dehe PM]]
-[[Category: Guerois, R]]
+[[Category: Geli V]]
-[[Category: Leulliot, N]]
+[[Category: Guerois R]]
-[[Category: Luciano, P]]
+[[Category: Leulliot N]]
-[[Category: Pamblanco, M]]
+[[Category: Luciano P]]
-[[Category: Quevillon-Cheruel, S]]
+[[Category: Pamblanco M]]
-[[Category: Rodriguez-Gil, A]]
+[[Category: Quevillon-Cheruel S]]
-[[Category: Salah, P]]
+[[Category: Rodriguez-Gil A]]
-[[Category: Sollier, J]]
+[[Category: Salah P]]
-[[Category: Tilbeurgh, H Van]]
+[[Category: Sollier J]]
-[[Category: Tordera, V]]
+[[Category: Tordera V]]
-[[Category: Tresaugues, L]]
+[[Category: Tresaugues L]]
-[[Category: Varlet, I]]
+[[Category: Van Tilbeurgh H]]
-[[Category: Zinn-Justin, S]]
+[[Category: Varlet I]]
-[[Category: Chromosomal protein]]
+[[Category: Zinn-Justin S]]
-[[Category: Histone methyltransferase]]
-[[Category: Methyltransferase]]
-[[Category: Nuclear protein]]
-[[Category: Rrm fold]]
-[[Category: Telomere]]
-[[Category: Transferase]]