OCA at 06:47, 23 May 2019

2019-05-23T06:47:44Z

←Older revision		Revision as of 06:47, 23 May 2019
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-	'''Unreleased structure'''

-	~~The entry~~ 6h1d is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of C21orf127-TRMT112 in complex with SAH==
		+	<StructureSection load='6h1d' size='340' side='right'caption='[[6h1d]], [[Resolution\|resolution]] 1.94Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6h1d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H1D FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=6h1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h1d OCA], [http://pdbe.org/6h1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h1d RCSB], [http://www.ebi.ac.uk/pdbsum/6h1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h1d ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/N6MT1_HUMAN N6MT1_HUMAN]] Methyltransferase that can methylate both proteins and DNA, and to a lower extent, arsenic (PubMed:18539146, PubMed:21193388, PubMed:30017583). Catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif (PubMed:18539146) (By similarity). Methylates ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated (PubMed:18539146, PubMed:20606008). Also acts as a N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)-methyladenosine) (PubMed:30017583). N(6)-methyladenosine (m6A) DNA is significantly enriched in exonic regions and is associated with gene transcriptional activation (PubMed:30017583). May also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid (PubMed:21193388, PubMed:25997655). It however only plays a limited role in arsenic metabolism compared with AS3MT (PubMed:25997655).[UniProtKB:Q6SKR2]<ref>PMID:18539146</ref> <ref>PMID:20606008</ref> <ref>PMID:21193388</ref> <ref>PMID:25997655</ref> <ref>PMID:30017583</ref> [[http://www.uniprot.org/uniprot/TR112_HUMAN TR112_HUMAN]] Acts as an activator of both rRNA/tRNA and protein methyltransferases (PubMed:25851604). Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA (PubMed:25851604). The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor (PubMed:18539146). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species (PubMed:20308323). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production (PubMed:25851604).<ref>PMID:18539146</ref> <ref>PMID:20308323</ref> <ref>PMID:25851604</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Histone lysine methylation is generally performed by SET domain methyltransferases and regulates chromatin structure and gene expression. Here, we identify human C21orf127 (HEMK2, N6AMT1, PrmC), a member of the seven-beta-strand family of putative methyltransferases, as a novel histone lysine methyltransferase. C21orf127 functions as an obligate heterodimer with TRMT112, writing the methylation mark on lysine 12 of histone H4 (H4K12) in vitro and in vivo. We characterized H4K12 recognition by solving the crystal structure of human C21orf127-TRMT112, hereafter termed 'lysine methyltransferase 9' (KMT9), in complex with S-adenosyl-homocysteine and H4K12me1 peptide. Additional analyses revealed enrichment for KMT9 and H4K12me1 at the promoters of numerous genes encoding cell cycle regulators and control of cell cycle progression by KMT9. Importantly, KMT9 depletion severely affects the proliferation of androgen receptor-dependent, as well as that of castration- and enzalutamide-resistant prostate cancer cells and xenograft tumors. Our data link H4K12 methylation with KMT9-dependent regulation of androgen-independent prostate tumor cell proliferation, thereby providing a promising paradigm for the treatment of castration-resistant prostate cancer.

-	~~Authors~~:	+	KMT9 monomethylates histone H4 lysine 12 and controls proliferation of prostate cancer cells.,Metzger E, Wang S, Urban S, Willmann D, Schmidt A, Offermann A, Allen A, Sum M, Obier N, Cottard F, Ulferts S, Preca BT, Hermann B, Maurer J, Greschik H, Hornung V, Einsle O, Perner S, Imhof A, Jung M, Schule R Nat Struct Mol Biol. 2019 May;26(5):361-371. doi: 10.1038/s41594-019-0219-9. Epub, 2019 May 6. PMID:31061526<ref>PMID:31061526</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6h1d" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Einsle, O]]
		+	[[Category: Hermann, B]]
		+	[[Category: Metzger, E]]
		+	[[Category: Peng, L]]
		+	[[Category: Schuele, R]]
		+	[[Category: Wang, S]]
		+	[[Category: Complex]]
		+	[[Category: Gene regulation]]
		+	[[Category: Histone methylation]]
		+	[[Category: Protein methyltransferase]]
		+	[[Category: Sah]]

OCA at 05:46, 20 March 2019

2019-03-20T05:46:44Z

←Older revision		Revision as of 05:46, 20 March 2019
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6h1d is ON HOLD	+	The entry 6h1d is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6h1d" [edit=sysop:move=sysop]

2018-07-18T05:54:10Z

Protected "6h1d" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:54, 18 July 2018

OCA: New page: '''Unreleased structure''' The entry 6h1d is ON HOLD Authors: Description: Category: Unreleased Structures

2018-07-18T05:54:06Z

New page: '''Unreleased structure''' The entry 6h1d is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6h1d is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]

6h1d - Revision history

OCA at 06:47, 23 May 2019

OCA at 05:46, 20 March 2019

OCA: Protected "6h1d" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 6h1d is ON HOLD Authors: Description: Category: Unreleased Structures