5e1o - Revision history

OCA at 12:27, 6 March 2024

2024-03-06T12:27:05Z

←Older revision		Revision as of 12:27, 6 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/NTM1A_HUMAN NTM1A_HUMAN] Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.<ref>PMID:20481588</ref> <ref>PMID:20668449</ref> <ref>PMID:24090352</ref>		[https://www.uniprot.org/uniprot/NTM1A_HUMAN NTM1A_HUMAN] Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.<ref>PMID:20481588</ref> <ref>PMID:20668449</ref> <ref>PMID:24090352</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	alpha-N-terminal methylation represents a highly conserved and prevalent post-translational modification, yet its biological function has remained largely speculative. The recent discovery of alpha-N-terminal methyltransferase 1 (NTMT1) and its physiological substrates propels the elucidation of a general role of alpha-N-terminal methylation in mediating DNA-binding ability of the modified proteins. The phenotypes, observed from both NTMT1 knockdown in breast cancer cell lines and knockout mouse models, suggest the potential involvement of alpha-N-terminal methylation in DNA damage response and cancer development. In this study, we report the first crystal structures of human NTMT1 in complex with cofactor S-adenosyl-L-homocysteine (SAH) and six substrate peptides, respectively, and reveal that NTMT1 contains two characteristic structural elements (a beta hairpin and an N-terminal extension) that contribute to its substrate specificity. Our complex structures, coupled with mutagenesis, binding, and enzymatic studies, also present the key elements involved in locking the consensus substrate motif XPK (X indicates any residue type other than D/E) into the catalytic pocket for alpha-N-terminal methylation and explain why NTMT1 prefers an XPK sequence motif. We propose a catalytic mechanism for alpha-N-terminal methylation. Overall, this study gives us the first glimpse of the molecular mechanism of alpha-N-terminal methylation and potentially contributes to the advent of therapeutic agents for human diseases associated with deregulated alpha-N-terminal methylation.
-
-	Structural basis for substrate recognition by the human N-terminal methyltransferase 1.,Dong C, Mao Y, Tempel W, Qin S, Li L, Loppnau P, Huang R, Min J Genes Dev. 2015 Nov 15;29(22):2343-8. doi: 10.1101/gad.270611.115. Epub 2015 Nov , 5. PMID:26543161<ref>PMID:26543161</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5e1o" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:09, 5 July 2023

2023-07-05T06:09:57Z

←Older revision		Revision as of 06:09, 5 July 2023
Line 3:		Line 3:
	<StructureSection load='5e1o' size='340' side='right'caption='[[5e1o]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5e1o' size='340' side='right'caption='[[5e1o]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5e1o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1O OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5E1O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5e1o]] is a 4 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=5E1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E1O FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S~~-~~ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>~~, ~~<scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>~~</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]] 2Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[5e1d\|5e1d]], [[5e2a\|5e2a]], [[5e1m\|5e1m]], [[5e2b\|5e2b]], [[5e1b\|5e1b]]~~<~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class="sblockDat"><span class~~='~~plainlinks~~'>~~[http://en.wikipedia.org/wiki/Protein_N-terminal_methyltransferase Protein N-terminal methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.244 2.1.1.244]~~ </~~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=5e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1o OCA], [https://pdbe.org/5e1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e1o RCSB], [https://www.ebi.ac.uk/pdbsum/5e1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1o ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1o OCA], [~~http~~://pdbe.org/5e1o PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5e1o RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5e1o PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1o ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NTM1A_HUMAN NTM1A_HUMAN]] Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.<ref>PMID:20481588</ref> <ref>PMID:20668449</ref> <ref>PMID:24090352</ref>	+	[https://www.uniprot.org/uniprot/NTM1A_HUMAN NTM1A_HUMAN] Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.<ref>PMID:20481588</ref> <ref>PMID:20668449</ref> <ref>PMID:24090352</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Protein N-terminal methyltransferase]]~~	+	[[Category: Arrowsmith CH]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Bountra C]]
-	[[Category: Bountra, C]]	+	[[Category: Dong C]]
-	[[Category: Dong, C]]	+	[[Category: Edwards AM]]
-	[[Category: Edwards~~, A M~~]]	+	[[Category: Min J]]
-	[[Category: Min, J]]	+	[[Category: Tempel W]]
-	~~[[Category: Structural genomic~~]]	+
-	[[Category: Tempel, W]]	+
-	~~[[Category: Methyl transferase]]~~	+
-	~~[[Category: Sgc]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:17, 15 April 2020

2020-04-15T08:17:44Z

←Older revision		Revision as of 08:17, 15 April 2020
Line 1:		Line 1:

	==Crystal structure of NTMT1 in complex with RPKRIA peptide==		==Crystal structure of NTMT1 in complex with RPKRIA peptide==
-	<StructureSection load='5e1o' size='340' side='right' caption='[[5e1o]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5e1o' size='340' side='right'caption='[[5e1o]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5e1o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1O OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5E1O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5e1o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E1O FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5e1d\|5e1d]], [[5e2a\|5e2a]], [[5e1m\|5e1m]], [[5e2b\|5e2b]], [[5e1b\|5e1b]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5e1d\|5e1d]], [[5e2a\|5e2a]], [[5e1m\|5e1m]], [[5e2b\|5e2b]], [[5e1b\|5e1b]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_N-terminal_methyltransferase Protein N-terminal methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.244 2.1.1.244] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_N-terminal_methyltransferase Protein N-terminal methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.244 2.1.1.244] </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=5e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1o OCA], [http://pdbe.org/5e1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1o RCSB], [http://www.ebi.ac.uk/pdbsum/5e1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1o ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1o OCA], [http://pdbe.org/5e1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1o RCSB], [http://www.ebi.ac.uk/pdbsum/5e1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1o ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Protein N-terminal methyltransferase]]		[[Category: Protein N-terminal methyltransferase]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]

OCA at 17:02, 18 August 2017

2017-08-18T17:02:16Z

←Older revision		Revision as of 17:02, 18 August 2017
Line 1:		Line 1:
		+
	==Crystal structure of NTMT1 in complex with RPKRIA peptide==		==Crystal structure of NTMT1 in complex with RPKRIA peptide==
	<StructureSection load='5e1o' size='340' side='right' caption='[[5e1o]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5e1o' size='340' side='right' caption='[[5e1o]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5e1d\|5e1d]], [[5e2a\|5e2a]], [[5e1m\|5e1m]], [[5e2b\|5e2b]], [[5e1b\|5e1b]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5e1d\|5e1d]], [[5e2a\|5e2a]], [[5e1m\|5e1m]], [[5e2b\|5e2b]], [[5e1b\|5e1b]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_N-terminal_methyltransferase Protein N-terminal methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.244 2.1.1.244] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_N-terminal_methyltransferase Protein N-terminal methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.244 2.1.1.244] </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=5e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1o OCA], [http://pdbe.org/5e1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1o RCSB], [http://www.ebi.ac.uk/pdbsum/5e1o PDBsum]</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=5e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1o OCA], [http://pdbe.org/5e1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1o RCSB], [http://www.ebi.ac.uk/pdbsum/5e1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1o ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 19:49, 30 November 2015

2015-11-30T19:49:51Z

←Older revision		Revision as of 19:49, 30 November 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of NTMT1 in complex with RPKRIA peptide==
		+	<StructureSection load='5e1o' size='340' side='right' caption='[[5e1o]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5e1o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E1O FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5e1d\|5e1d]], [[5e2a\|5e2a]], [[5e1m\|5e1m]], [[5e2b\|5e2b]], [[5e1b\|5e1b]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_N-terminal_methyltransferase Protein N-terminal methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.244 2.1.1.244] </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=5e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1o OCA], [http://pdbe.org/5e1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1o RCSB], [http://www.ebi.ac.uk/pdbsum/5e1o PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NTM1A_HUMAN NTM1A_HUMAN]] Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.<ref>PMID:20481588</ref> <ref>PMID:20668449</ref> <ref>PMID:24090352</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	alpha-N-terminal methylation represents a highly conserved and prevalent post-translational modification, yet its biological function has remained largely speculative. The recent discovery of alpha-N-terminal methyltransferase 1 (NTMT1) and its physiological substrates propels the elucidation of a general role of alpha-N-terminal methylation in mediating DNA-binding ability of the modified proteins. The phenotypes, observed from both NTMT1 knockdown in breast cancer cell lines and knockout mouse models, suggest the potential involvement of alpha-N-terminal methylation in DNA damage response and cancer development. In this study, we report the first crystal structures of human NTMT1 in complex with cofactor S-adenosyl-L-homocysteine (SAH) and six substrate peptides, respectively, and reveal that NTMT1 contains two characteristic structural elements (a beta hairpin and an N-terminal extension) that contribute to its substrate specificity. Our complex structures, coupled with mutagenesis, binding, and enzymatic studies, also present the key elements involved in locking the consensus substrate motif XPK (X indicates any residue type other than D/E) into the catalytic pocket for alpha-N-terminal methylation and explain why NTMT1 prefers an XPK sequence motif. We propose a catalytic mechanism for alpha-N-terminal methylation. Overall, this study gives us the first glimpse of the molecular mechanism of alpha-N-terminal methylation and potentially contributes to the advent of therapeutic agents for human diseases associated with deregulated alpha-N-terminal methylation.

-	~~The entry 5e1o is ON HOLD~~	+	Structural basis for substrate recognition by the human N-terminal methyltransferase 1.,Dong C, Mao Y, Tempel W, Qin S, Li L, Loppnau P, Huang R, Min J Genes Dev. 2015 Nov 15;29(22):2343-8. doi: 10.1101/gad.270611.115. Epub 2015 Nov , 5. PMID:26543161<ref>PMID:26543161</ref>

-	~~Authors: Dong~~, C.~~, Tempel, W~~.~~, Bountra, C~~., Arrowsmith, C.H., ~~Edwards, A.M., Min, J., Structural Genomics Consortium (SGC)~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal structure of NTMT1 in complex with RPKRIA peptide~~	+	<div class="pdbe-citations 5e1o" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Unreleased Structures~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Protein N-terminal methyltransferase]]
		+	[[Category: Arrowsmith, C H]]
		+	[[Category: Bountra, C]]
		+	[[Category: Dong, C]]
		+	[[Category: Edwards, A M]]
	[[Category: Min, J]]		[[Category: Min, J]]
-	[[Category: ~~Bountra, C~~]]	+	[[Category: Structural genomic]]
	[[Category: Tempel, W]]		[[Category: Tempel, W]]
-	[[Category: ~~Arrowsmith, C.H~~]]	+	[[Category: Methyl transferase]]
-	[[Category: ~~Dong, C~~]]	+	[[Category: Sgc]]
-	[[Category: ~~Edwards, A.M]]~~	+	[[Category: Transferase]]
-	~~[[Category: Structural Genomics Consortium (Sgc)~~]]	+

OCA: Protected "5e1o" [edit=sysop:move=sysop]

2015-10-07T12:50:42Z

Protected "5e1o" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:50, 7 October 2015

OCA: New page: '''Unreleased structure''' The entry 5e1o is ON HOLD Authors: Dong, C., Tempel, W., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Min, J., Structural Genomics Consortium (SGC) Descript...

2015-10-07T12:50:39Z

New page: '''Unreleased structure''' The entry 5e1o is ON HOLD Authors: Dong, C., Tempel, W., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Min, J., Structural Genomics Consortium (SGC) Descript...

New page

'''Unreleased structure'''

The entry 5e1o is ON HOLD

Authors: Dong, C., Tempel, W., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Min, J., Structural Genomics Consortium (SGC)

Description: Crystal structure of NTMT1 in complex with RPKRIA peptide
[[Category: Unreleased Structures]]
[[Category: Min, J]]
[[Category: Bountra, C]]
[[Category: Tempel, W]]
[[Category: Arrowsmith, C.H]]
[[Category: Dong, C]]
[[Category: Edwards, A.M]]
[[Category: Structural Genomics Consortium (Sgc)]]