1muf: Difference between revisions
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==Structure of histone H3 K4-specific methyltransferase SET7/9== | ==Structure of histone H3 K4-specific methyltransferase SET7/9== | ||
<StructureSection load='1muf' size='340' side='right' caption='[[1muf]], [[Resolution|resolution]] 2.26Å' scene=''> | <StructureSection load='1muf' size='340' side='right'caption='[[1muf]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1muf]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1muf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MUF FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1muf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1muf OCA], [https://pdbe.org/1muf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1muf RCSB], [https://www.ebi.ac.uk/pdbsum/1muf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1muf ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1muf_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1muf_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 33: | Line 31: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Devarakonda | [[Category: Devarakonda S]] | ||
[[Category: Harp | [[Category: Harp JM]] | ||
[[Category: Jacobs | [[Category: Jacobs SA]] | ||
[[Category: Khorasanizadeh | [[Category: Khorasanizadeh S]] | ||
[[Category: Kim | [[Category: Kim Y]] | ||
[[Category: Rastinejad | [[Category: Rastinejad F]] | ||
Latest revision as of 03:15, 21 November 2024
Structure of histone H3 K4-specific methyltransferase SET7/9Structure of histone H3 K4-specific methyltransferase SET7/9
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe SET domain contains the catalytic center of lysine methyltransferases that target the N-terminal tails of histones and regulate chromatin function. Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy). A knot within the SET domain helps form the methyltransferase active site, where AdoHcy binds and lysine methylation is likely to occur. A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain. The active site of the SET domain is constructed on a knot.,Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S Nat Struct Biol. 2002 Nov;9(11):833-8. PMID:12389038[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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