4pgf - Revision history

OCA at 07:16, 27 September 2023

2023-09-27T07:16:53Z

← Older revision		Revision as of 07:16, 27 September 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pgf]] is a 2 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=4PGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PGF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pgf]] is a 2 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=4PGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PGF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 2.59Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [https://pdbe.org/4pgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [https://www.ebi.ac.uk/pdbsum/4pgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgf ProSAT]</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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [https://pdbe.org/4pgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [https://www.ebi.ac.uk/pdbsum/4pgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgf ProSAT]</span></td></tr>
	</table>		</table>

OCA at 13:01, 1 February 2023

2023-02-01T13:01:09Z

← Older revision		Revision as of 13:01, 1 February 2023
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	==The structure of mono-acetylated SAHH==		==The structure of mono-acetylated SAHH==
	<StructureSection load='4pgf' size='340' side='right' caption='[[4pgf]], [[Resolution\|resolution]] 2.59Å' scene=''>		<StructureSection load='4pgf' size='340' side='right'caption='[[4pgf]], [[Resolution\|resolution]] 2.59Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pgf]] is a 2 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=4PGF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4PGF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pgf]] is a 2 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=4PGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PGF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, ~~<scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [https://pdbe.org/4pgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [https://www.ebi.ac.uk/pdbsum/4pgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgf ProSAT]</span></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pfj\|4pfj]]</td></tr>~~
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AHCY~~, ~~SAHH ([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/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1]~~ </~~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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [~~http~~://pdbe.org/4pgf PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4pgf PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[~~[http~~://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:[~~http~~://omim.org/entry/613752 613752]]. A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy.<ref>PMID:15024124</ref> <ref>PMID:16736098</ref> <ref>PMID:19177456</ref> <ref>PMID:20852937</ref>		[https://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN] Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:[https://omim.org/entry/613752 613752]. A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy.<ref>PMID:15024124</ref> <ref>PMID:16736098</ref> <ref>PMID:19177456</ref> <ref>PMID:20852937</ref>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.<ref>PMID:12590576</ref>		[https://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.<ref>PMID:12590576</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Adenosylhomocysteinase~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Human~~]]		[[Category: Large Structures]]
	[[Category: Cole~~, P A~~]]		[[Category: Cole PA]]
	[[Category: Kavran~~, J M~~]]		[[Category: Kavran JM]]
	[[Category: Leahy~~, D J~~]]		[[Category: Leahy DJ]]
	[[Category: Wang, Y]]		[[Category: Wang Y]]
	~~[[Category: Hydrolase]]~~
	~~[[Category: Hydrolyase acetylation sahh semi-synthetic~~]]

OCA at 08:40, 22 November 2017

2017-11-22T08:40:18Z

← Older revision		Revision as of 08:40, 22 November 2017
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	<StructureSection load='4pgf' size='340' side='right' caption='[[4pgf]], [[Resolution\|resolution]] 2.59Å' scene=''>		<StructureSection load='4pgf' size='340' side='right' caption='[[4pgf]], [[Resolution\|resolution]] 2.59Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pgf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PGF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PGF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pgf]] is a 2 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=4PGF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PGF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pfj\|4pfj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pfj\|4pfj]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AHCY, SAHH ([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/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [http://pdbe.org/4pgf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [http://www.ebi.ac.uk/pdbsum/4pgf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgf ProSAT]</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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [http://pdbe.org/4pgf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [http://www.ebi.ac.uk/pdbsum/4pgf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgf ProSAT]</span></td></tr>
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	</StructureSection>		</StructureSection>
	[[Category: Adenosylhomocysteinase]]		[[Category: Adenosylhomocysteinase]]
			[[Category: Human]]
	[[Category: Cole, P A]]		[[Category: Cole, P A]]
	[[Category: Kavran, J M]]		[[Category: Kavran, J M]]

OCA at 09:24, 11 August 2016

2016-08-11T09:24:53Z

← Older revision		Revision as of 09:24, 11 August 2016
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	==The structure of mono-acetylated SAHH==		==The structure of mono-acetylated SAHH==
	<StructureSection load='4pgf' size='340' side='right' caption='[[4pgf]], [[Resolution\|resolution]] 2.59Å' scene=''>		<StructureSection load='4pgf' size='340' side='right' caption='[[4pgf]], [[Resolution\|resolution]] 2.59Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pfj\|4pfj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pfj\|4pfj]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [http://www.ebi.ac.uk/pdbsum/4pgf 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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [http://pdbe.org/4pgf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [http://www.ebi.ac.uk/pdbsum/4pgf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4pgf" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:55, 19 November 2014

2014-11-19T10:55:35Z

← Older revision		Revision as of 10:55, 19 November 2014
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	</StructureSection>		</StructureSection>
	[[Category: Adenosylhomocysteinase]]		[[Category: Adenosylhomocysteinase]]
	[[Category: Cole, P A.]]		[[Category: Cole, P A]]
	[[Category: Kavran, J M.]]		[[Category: Kavran, J M]]
	[[Category: Leahy, D J.]]		[[Category: Leahy, D J]]
	[[Category: Wang, Y.]]		[[Category: Wang, Y]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Hydrolyase acetylation sahh semi-synthetic]]		[[Category: Hydrolyase acetylation sahh semi-synthetic]]

OCA at 05:57, 8 October 2014

2014-10-08T05:57:53Z

← Older revision		Revision as of 05:57, 8 October 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pgf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PGF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PGF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pgf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PGF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PGF FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pfj\|4pfj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pfj\|4pfj]]</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [http://www.ebi.ac.uk/pdbsum/4pgf 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=4pgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pgf RCSB], [http://www.ebi.ac.uk/pdbsum/4pgf PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:[http://omim.org/entry/613752 613752]]. A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy.<ref>PMID:15024124</ref> <ref>PMID:16736098</ref> <ref>PMID:19177456</ref> <ref>PMID:20852937</ref>		[[http://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:[http://omim.org/entry/613752 613752]]. A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy.<ref>PMID:15024124</ref> <ref>PMID:16736098</ref> <ref>PMID:19177456</ref> <ref>PMID:20852937</ref>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.<ref>PMID:12590576</ref>		[[http://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN]] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.<ref>PMID:12590576</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			S-adenosylhomocysteine hydrolase (SAHH) is an NAD+-dependent tetrameric enzyme that catalyzes the breakdown of S-adenosylhomocysteine to adenosine and homocysteine and is important in cell growth and the regulation of gene expression. Loss of SAHH function can result in global inhibition of cellular methyltransferase enzymes because of high levels of S-adenosylhomocysteine. Prior proteomics studies have identified two SAHH acetylation sites at Lys-401 and Lys-408 but the impact of these post-translational modifications has not yet been determined. Here we use expressed protein ligation to produce semisynthetic SAHH acetylated at Lys-401 and Lys-408 and show that modification of either position negatively impacts the catalytic activity of SAHH. X-ray crystal structures of 408-acetylated-SAHH and dually acetylated SAHH have been determined and reveal perturbations in the C-terminal hydrogen bonding patterns, a region of the protein important for NAD+ binding. These crystal structures along with mutagenesis data suggest that such hydrogen bond perturbations are responsible for SAHH catalytic inhibition by acetylation. These results suggest how increased acetylation of SAHH may globally influence cellular methylation patterns.

			Regulation of S-Adenosylhomocysteine Hydrolase by Lysine Acetylation.,Wang Y, Kavran JM, Chen Z, Karukurichi KR, Leahy DJ, Cole PA J Biol Chem. 2014 Sep 23. pii: jbc.M114.597153. PMID:25248746<ref>PMID:25248746</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 00:26, 2 October 2014

2014-10-02T00:26:00Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==The structure of mono-acetylated SAHH==
+<StructureSection load='4pgf' size='340' side='right' caption='[[4pgf]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
-The entry 4pgf is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4pgf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PGF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PGF FirstGlance]. <br>
-Authors: Kavran, J.M., Wang, Y., Cole, P.A., Leahy, D.J.
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br>
+<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
-Description:
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pfj|4pfj]]</td></tr>

OCA at 07:58, 24 September 2014

2014-09-24T07:58:54Z

← Older revision		Revision as of 07:58, 24 September 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4pgf is ON HOLD		The entry 4pgf is ON HOLD until Paper Publication

	Authors: Kavran, J.M., Wang, Y., Cole, P.A., Leahy, D.J.		Authors: Kavran, J.M., Wang, Y., Cole, P.A., Leahy, D.J.

	Description:		Description:

OCA: Protected "4pgf" [edit=sysop:move=sysop]

2014-05-07T07:45:27Z

Protected "4pgf" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:45, 7 May 2014
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4pgf is ON HOLD Authors: Kavran, J.M., Wang, Y., Cole, P.A., Leahy, D.J. Description:

2014-05-07T07:45:25Z

New page: '''Unreleased structure''' The entry 4pgf is ON HOLD Authors: Kavran, J.M., Wang, Y., Cole, P.A., Leahy, D.J. Description:

New page

'''Unreleased structure'''

The entry 4pgf is ON HOLD

Authors: Kavran, J.M., Wang, Y., Cole, P.A., Leahy, D.J.

Description: