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6ago

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Revision as of 07:26, 23 May 2019

Crystal structure of MRG15-ASH1L Histone methyltransferase complex

Structural highlights

6ago is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	ASH1L, KIAA1420, KMT2H (HUMAN), MORF4L1, MRG15, FWP006, HSPC008, HSPC061, PP368 (HUMAN)
Activity:	Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ASH1L_HUMAN] Histone methyltransferase specifically methylating 'Lys-36' of histone H3 (H3K36me).^[1]

Publication Abstract from PubMed

Human ASH1L is the catalytic subunit of the conserved histone methyltransferase (HMTase) complex AMC that dimethylates lysine 36 in histone H3 (H3K36me2) to promote gene transcription in mammals and flies. Unlike AMC, ASH1L alone shows poor catalytic activity, because access to its substrate binding pocket is blocked by an autoinhibitory loop (AI loop) from the postSET domain. We report the crystal structure of the minimal catalytic active AMC complex containing ASH1L and its partner subunit MRG15. The structure reveals how binding of the MRG domain of MRG15 to a conserved FxLP motif in ASH1L results in the displacement of the AI loop to permit substrates to access the catalytic pocket of the ASH1L SET domain. Together, ASH1L activation by MRG15 therefore represents a delicate regulatory mechanism for how a cofactor activates an SET domain HMTase by releasing autoinhibition.

Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop.,Lee Y, Yoon E, Cho S, Schmahling S, Muller J, Song JJ Structure. 2019 Feb 9. pii: S0969-2126(19)30016-4. doi:, 10.1016/j.str.2019.01.016. PMID:30827841^[2]

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

References

↑ An S, Yeo KJ, Jeon YH, Song JJ. Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. J Biol Chem. 2011 Mar 11;286(10):8369-74. Epub 2011 Jan 14. PMID:21239497 doi:10.1074/jbc.M110.203380
↑ Lee Y, Yoon E, Cho S, Schmahling S, Muller J, Song JJ. Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop. Structure. 2019 Feb 9. pii: S0969-2126(19)30016-4. doi:, 10.1016/j.str.2019.01.016. PMID:30827841 doi:http://dx.doi.org/10.1016/j.str.2019.01.016

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/6ago"

@@ Line 3: / Line 3: @@
 <StructureSection load='6ago' size='340' side='right'caption='[[6ago]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ago]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AGO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ago]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AGO FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASH1L, KIAA1420, KMT2H ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MORF4L1, MRG15, FWP006, HSPC008, HSPC061, PP368 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></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=6ago FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ago OCA], [http://pdbe.org/6ago PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ago RCSB], [http://www.ebi.ac.uk/pdbsum/6ago PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ago ProSAT]</span></td></tr>
@@ Line 24: / Line 25: @@
 </StructureSection>
 [[Category: Histone-lysine N-methyltransferase]]
+[[Category: Human]]
 [[Category: Large Structures]]
 [[Category: Lee, Y]]

6ago

From Proteopedia

Revision as of 07:26, 23 May 2019

Crystal structure of MRG15-ASH1L Histone methyltransferase complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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