3ond - Revision history

OCA at 09:42, 6 September 2023

2023-09-06T09:42:15Z

←Older revision		Revision as of 09:42, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3ond' size='340' side='right'caption='[[3ond]], [[Resolution\|resolution]] 1.17Å' scene=''>		<StructureSection load='3ond' size='340' side='right'caption='[[3ond]], [[Resolution\|resolution]] 1.17Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ond]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~European_yellow_lupine European yellow lupine~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OND FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ond]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OND 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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.17Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a7a\|1a7a]], [[1b3r\|1b3r]], [[1v8b\|1v8b]], [[3ce6\|3ce6]], [[3one\|3one]], [[3onf\|3onf]]</div></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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SAHH, SHH, shh-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3873 European yellow lupine])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [https://pdbe.org/3ond PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [https://www.ebi.ac.uk/pdbsum/3ond PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ond 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=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [https://pdbe.org/3ond PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [https://www.ebi.ac.uk/pdbsum/3ond PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ond ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU]] 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 (By similarity).	+	[https://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU] 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 (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Adenosylhomocysteinase]]
-	[[Category: European yellow lupine]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Brzezinski, K~~]]	+	[[Category: Lupinus luteus]]
-	[[Category: ~~Jaskolski, M~~]]	+	[[Category: Brzezinski K]]
-	[[Category: ~~Enzyme-substrate complex]]~~	+	[[Category: Jaskolski M]]
-	~~[[Category: Nad cofactor]]~~	+
-	~~[[Category: Plant protein]]~~	+
-	~~[[Category: Regulation of sam-dependent methylation reaction~~]]	+

OCA at 10:49, 18 May 2022

2022-05-18T10:49:52Z

←Older revision		Revision as of 10:49, 18 May 2022
Line 1:		Line 1:

	==Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine==		==Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine==
-	<StructureSection load='3ond' size='340' side='right' caption='[[3ond]], [[Resolution\|resolution]] 1.17Å' scene=''>	+	<StructureSection load='3ond' size='340' side='right'caption='[[3ond]], [[Resolution\|resolution]] 1.17Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ond]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~European_yellow_lupin~~ European yellow ~~lupin~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3OND FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ond]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_yellow_lupine European yellow lupine]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OND 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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a7a\|1a7a]], [[1b3r\|1b3r]], [[1v8b\|1v8b]], [[3ce6\|3ce6]], [[3one\|3one]], [[3onf\|3onf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a7a\|1a7a]], [[1b3r\|1b3r]], [[1v8b\|1v8b]], [[3ce6\|3ce6]], [[3one\|3one]], [[3onf\|3onf]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SAHH, SHH, shh-1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3873 European yellow ~~lupin~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SAHH, SHH, shh-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3873 European yellow lupine])</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'>[https://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [https://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=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [~~http~~://pdbe.org/3ond PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ond PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ond 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=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [https://pdbe.org/3ond PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [https://www.ebi.ac.uk/pdbsum/3ond PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ond ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU]] 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 (By similarity).	+	[[https://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU]] 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 (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Adenosylhomocysteinase]]		[[Category: Adenosylhomocysteinase]]
-	[[Category: European yellow ~~lupin~~]]	+	[[Category: European yellow lupine]]
		+	[[Category: Large Structures]]
	[[Category: Brzezinski, K]]		[[Category: Brzezinski, K]]
	[[Category: Jaskolski, M]]		[[Category: Jaskolski, M]]

OCA at 15:33, 5 August 2016

2016-08-05T15:33:58Z

←Older revision		Revision as of 15:33, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine==		==Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine==
	<StructureSection load='3ond' size='340' side='right' caption='[[3ond]], [[Resolution\|resolution]] 1.17Å' scene=''>		<StructureSection load='3ond' size='340' side='right' caption='[[3ond]], [[Resolution\|resolution]] 1.17Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SAHH, SHH, shh-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3873 European yellow lupin])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SAHH, SHH, shh-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3873 European yellow lupin])</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=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [http://www.ebi.ac.uk/pdbsum/3ond 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=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [http://pdbe.org/3ond PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [http://www.ebi.ac.uk/pdbsum/3ond PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ond ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3ond" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 19:56, 25 December 2014

2014-12-25T19:56:55Z

←Older revision		Revision as of 19:56, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3ond\| PDB=3ond \| SCENE= }}~~	+	==Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine==
-	===Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine===	+	<StructureSection load='3ond' size='340' side='right' caption='[[3ond]], [[Resolution\|resolution]] 1.17Å' scene=''>
-	~~{{ABSTRACT_PUBMED_22349223}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3ond]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_yellow_lupin European yellow lupin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OND FirstGlance]. <br>
-	==Function==	+	</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a7a\|1a7a]], [[1b3r\|1b3r]], [[1v8b\|1v8b]], [[3ce6\|3ce6]], [[3one\|3one]], [[3onf\|3onf]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SAHH, SHH, shh-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3873 European yellow lupin])</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=3ond FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ond OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ond RCSB], [http://www.ebi.ac.uk/pdbsum/3ond PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU]] 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 (By similarity).		[[http://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU]] 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 (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	S-Adenosyl-L-homocysteine hydrolase (SAHase) catalyzes the reversible breakdown of S-adenosyl-L-homocysteine (SAH) to adenosine and homocysteine. SAH is formed in methylation reactions that utilize S-adenosyl-L-methionine (SAM) as a methyl donor. By removing the SAH byproduct, SAHase serves as a major regulator of SAM-dependent biological methylation reactions. Here, the first crystal structure of SAHase of plant origin, that from the legume yellow lupin (LlSAHase), is presented. Structures have been determined at high resolution for three complexes of the enzyme: those with a reaction byproduct/substrate (adenosine), with its nonoxidizable analog (cordycepin) and with a product of inhibitor cleavage (adenine). In all three cases the enzyme has a closed conformation. A sodium cation is found near the active site, coordinated by residues from a conserved loop that hinges domain movement upon reactant binding. An insertion segment that is present in all plant SAHases is located near a substrate-pocket access channel and participates in its formation. In contrast to mammalian and bacterial SAHases, the channel is open when adenosine or cordycepin is bound and is closed in the adenine complex. In contrast to SAHases from other organisms, which are active as tetramers, the plant enzyme functions as a homodimer in solution.

-	~~==About this Structure==~~	+	High-resolution structures of complexes of plant S-adenosyl-L-homocysteine hydrolase (Lupinus luteus).,Brzezinski K, Dauter Z, Jaskolski M Acta Crystallogr D Biol Crystallogr. 2012 Mar;68(Pt 3):218-31. Epub 2012 Feb 7. PMID:22349223<ref>PMID:22349223</ref>
-	~~[[3ond]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/European_yellow_lupin European yellow lupin]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=3OND OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[S-adenosylhomocysteine hydrolase\|S-adenosylhomocysteine hydrolase]]		*[[S-adenosylhomocysteine hydrolase\|S-adenosylhomocysteine hydrolase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:022349223</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Adenosylhomocysteinase]]		[[Category: Adenosylhomocysteinase]]
	[[Category: European yellow lupin]]		[[Category: European yellow lupin]]
-	[[Category: Brzezinski, K.]]	+	[[Category: Brzezinski, K]]
-	[[Category: Jaskolski, M.]]	+	[[Category: Jaskolski, M]]
	[[Category: Enzyme-substrate complex]]		[[Category: Enzyme-substrate complex]]
	[[Category: Nad cofactor]]		[[Category: Nad cofactor]]
	[[Category: Plant protein]]		[[Category: Plant protein]]
	[[Category: Regulation of sam-dependent methylation reaction]]		[[Category: Regulation of sam-dependent methylation reaction]]

OCA at 15:18, 19 February 2014

2014-02-19T15:18:58Z

←Older revision		Revision as of 15:18, 19 February 2014
Line 1:		Line 1:
-	[[Image:3ond.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3ond", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3ond\| PDB=3ond \| SCENE= }}		{{STRUCTURE_3ond\| PDB=3ond \| SCENE= }}
-
	===Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine===		===Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine===
		+	{{ABSTRACT_PUBMED_22349223}}

		+	==Function==
		+	[[http://www.uniprot.org/uniprot/SAHH_LUPLU SAHH_LUPLU]] 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 (By similarity).

-	~~<!--~~	+	==About this Structure==
-	~~The line below~~ this ~~paragraph, {{ABSTRACT_PUBMED_22349223}}, adds the Publication Abstract to the page~~	+	[[3ond]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_yellow_lupin European yellow lupin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA].
-	~~(as it appears on PubMed at~~ http://~~www~~.~~pubmed~~.~~gov), where 22349223~~ is ~~the PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_22349223}}~~	+

-	==~~About this Structure~~==	+	==See Also==
-	[[~~3ond~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA].	+	*[[S-adenosylhomocysteine hydrolase\|S-adenosylhomocysteine hydrolase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:022349223</ref><~~ref~~ group="xtra"~~>PMID:018607106<~~/ref><ref group="xtra">PMID:011732617</ref><ref group="xtra">PMID:009586999</ref><ref group="xtra">PMID:010387078</ref><ref group="xtra">PMID:015476817</ref><ref group="xtra">PMID:018815415</ref><ref group="xtra">PMID:015579379</ref><references ~~group="xtra"~~/>	+	<ref group="xtra">PMID:022349223</ref><references group="xtra"/><references/>
	[[Category: Adenosylhomocysteinase]]		[[Category: Adenosylhomocysteinase]]
-	[[Category: ~~Lupinus luteus~~]]	+	[[Category: European yellow lupin]]
	[[Category: Brzezinski, K.]]		[[Category: Brzezinski, K.]]
	[[Category: Jaskolski, M.]]		[[Category: Jaskolski, M.]]

OCA at 05:23, 4 April 2012

2012-04-04T05:23:58Z

←Older revision		Revision as of 05:23, 4 April 2012
Line 1:		Line 1:
-	[[Image:3ond.~~jpg~~\|left\|200px]]	+	[[Image:3ond.png\|left\|200px]]

	<!--		<!--
Line 13:		Line 13:

	<!--		<!--
-	The line below this paragraph, {{~~ABSTRACT_PUBMED_18607106~~}}, adds the Publication Abstract to the page	+	The line below this paragraph, {{ABSTRACT_PUBMED_22349223}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where ~~18607106~~ is the PubMed ID number.	+	(as it appears on PubMed at http://www.pubmed.gov), where 22349223 is the PubMed ID number.
	-->		-->
-	{{~~ABSTRACT_PUBMED_18607106~~}}	+	{{ABSTRACT_PUBMED_22349223}}

	==About this Structure==		==About this Structure==
Line 22:		Line 22:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:018607106</ref><ref group="xtra">PMID:011732617</ref><ref group="xtra">PMID:009586999</ref><ref group="xtra">PMID:010387078</ref><ref group="xtra">PMID:015476817</ref><ref group="xtra">PMID:018815415</ref><ref group="xtra">PMID:015579379</ref><references group="xtra"/>	+	<ref group="xtra">PMID:022349223</ref><ref group="xtra">PMID:018607106</ref><ref group="xtra">PMID:011732617</ref><ref group="xtra">PMID:009586999</ref><ref group="xtra">PMID:010387078</ref><ref group="xtra">PMID:015476817</ref><ref group="xtra">PMID:018815415</ref><ref group="xtra">PMID:015579379</ref><references group="xtra"/>
	[[Category: Adenosylhomocysteinase]]		[[Category: Adenosylhomocysteinase]]
	[[Category: Lupinus luteus]]		[[Category: Lupinus luteus]]

OCA at 06:55, 31 August 2011

2011-08-31T06:55:01Z

←Older revision		Revision as of 06:55, 31 August 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3ond.jpg\|left\|200px]]

-	The ~~entry 3ond~~ is ~~ON HOLD~~ ~~until Aug 28 2012~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3ond", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3ond\| PDB=3ond \| SCENE= }}

-	~~Authors: Brzezinski, K., Jaskolski, M.~~	+	===Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine===

-	~~Description~~: ~~Crystal~~ structure of Lupinus luteus S-~~adenosyl~~-~~L-homocysteine hydrolase in~~ complex ~~with adenosine~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_18607106}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18607106 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18607106}}
		+
		+	==About this Structure==
		+	[[3ond]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OND OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:018607106</ref><ref group="xtra">PMID:011732617</ref><ref group="xtra">PMID:009586999</ref><ref group="xtra">PMID:010387078</ref><ref group="xtra">PMID:015476817</ref><ref group="xtra">PMID:018815415</ref><ref group="xtra">PMID:015579379</ref><references group="xtra"/>
		+	[[Category: Adenosylhomocysteinase]]
		+	[[Category: Lupinus luteus]]
		+	[[Category: Brzezinski, K.]]
		+	[[Category: Jaskolski, M.]]
		+	[[Category: Enzyme-substrate complex]]
		+	[[Category: Nad cofactor]]
		+	[[Category: Plant protein]]
		+	[[Category: Regulation of sam-dependent methylation reaction]]

OCA at 05:22, 10 August 2011

2011-08-10T05:22:57Z

←Older revision		Revision as of 05:22, 10 August 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3ond is ON HOLD until ~~Paper Publication~~	+	The entry 3ond is ON HOLD until Aug 28 2012

	Authors: Brzezinski, K., Jaskolski, M.		Authors: Brzezinski, K., Jaskolski, M.

	Description: Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine		Description: Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine

OCA: Protected "3ond" [edit=sysop:move=sysop]

2011-02-09T05:44:41Z

Protected "3ond" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:44, 9 February 2011

OCA at 05:44, 9 February 2011

2011-02-09T05:44:40Z

←Older revision		Revision as of 05:44, 9 February 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3ond is ON HOLD	+	The entry 3ond is ON HOLD until Paper Publication

	Authors: Brzezinski, K., Jaskolski, M.		Authors: Brzezinski, K., Jaskolski, M.

	Description: Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine		Description: Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 15 10:37:40 2010''