1o93 - Revision history

OCA at 12:31, 13 December 2023

2023-12-13T12:31:54Z

←Older revision		Revision as of 12:31, 13 December 2023
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	<StructureSection load='1o93' size='340' side='right'caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>		<StructureSection load='1o93' size='340' side='right'caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O93 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O93 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 3.49Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [https://pdbe.org/1o93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [https://www.ebi.ac.uk/pdbsum/1o93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o93 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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [https://pdbe.org/1o93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [https://www.ebi.ac.uk/pdbsum/1o93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o93 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/METK1_RAT METK1_RAT]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.	+	[https://www.uniprot.org/uniprot/METK1_RAT METK1_RAT] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 31:

	==See Also==		==See Also==
-	*[[Methionine adenosyltransferase\|Methionine adenosyltransferase]]
	*[[S-adenosylmethionine synthetase 3D structures\|S-adenosylmethionine synthetase 3D structures]]		*[[S-adenosylmethionine synthetase 3D structures\|S-adenosylmethionine synthetase 3D structures]]
	== References ==		== References ==
Line 38:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Methionine adenosyltransferase~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Gonzalez, B]]	+	[[Category: Gonzalez B]]
-	[[Category: Hermoso~~, J A~~]]	+	[[Category: Hermoso JA]]
-	[[Category: Pajares~~, M A~~]]	+	[[Category: Pajares MA]]
-	[[Category: Sanz-Aparicio, J]]	+	[[Category: Sanz-Aparicio J]]
-	~~[[Category: Adenosyltransferase]]~~	+
-	~~[[Category: Methionine and atp binding]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 12:08, 27 April 2022

2022-04-27T12:08:57Z

←Older revision		Revision as of 12:08, 27 April 2022
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	<StructureSection load='1o93' size='340' side='right'caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>		<StructureSection load='1o93' size='340' side='right'caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1O93 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O93 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [~~http~~://pdbe.org/1o93 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1o93 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1o93 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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [https://pdbe.org/1o93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [https://www.ebi.ac.uk/pdbsum/1o93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o93 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/METK1_RAT METK1_RAT]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.	+	[[https://www.uniprot.org/uniprot/METK1_RAT METK1_RAT]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[~~SAM~~ synthetase\|~~SAM~~ synthetase]]	+	*[[Methionine adenosyltransferase\|Methionine adenosyltransferase]]
		+	*[[S-adenosylmethionine synthetase 3D structures\|S-adenosylmethionine synthetase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:05, 22 July 2020

2020-07-22T12:05:01Z

←Older revision		Revision as of 12:05, 22 July 2020
Line 1:		Line 1:

	==Methionine Adenosyltransferase complexed with ATP and a L-methionine analogue==		==Methionine Adenosyltransferase complexed with ATP and a L-methionine analogue==
-	<StructureSection load='1o93' size='340' side='right' caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>	+	<StructureSection load='1o93' size='340' side='right'caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1O93 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O93 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://pdbe.org/1o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o93 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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://pdbe.org/1o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o93 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Methionine adenosyltransferase]]		[[Category: Methionine adenosyltransferase]]
	[[Category: Gonzalez, B]]		[[Category: Gonzalez, B]]

OCA at 05:42, 30 May 2018

2018-05-30T05:42:33Z

←Older revision		Revision as of 05:42, 30 May 2018
Line 1:		Line 1:

-	==Methionine Adenosyltransferase complexed with ATP and a L-methionine ~~analogous~~==	+	==Methionine Adenosyltransferase complexed with ATP and a L-methionine analogue==
	<StructureSection load='1o93' size='340' side='right' caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>		<StructureSection load='1o93' size='340' side='right' caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1o93" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1o93" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[SAM synthetase\|SAM synthetase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:02, 7 February 2018

2018-02-07T07:02:34Z

←Older revision		Revision as of 07:02, 7 February 2018
Line 1:		Line 1:
-	==~~METHIONINE ADENOSYLTRANSFERASE COMPLEXED WITH~~ ATP ~~AND A~~ L-~~METHIONINE ANALOGOUS~~==	+
		+	==Methionine Adenosyltransferase complexed with ATP and a L-methionine analogous==
	<StructureSection load='1o93' size='340' side='right' caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>		<StructureSection load='1o93' size='340' side='right' caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://pdbe.org/1o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://pdbe.org/1o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o93 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o9/1o93_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o9/1o93_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1o93" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1o93" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[SAM synthetase\|SAM synthetase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:17, 8 February 2016

2016-02-08T14:17:48Z

←Older revision		Revision as of 14:17, 8 February 2016
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o93 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 12:23, 10 September 2015

2015-09-10T12:23:27Z

←Older revision		Revision as of 12:23, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1o93' size='340' side='right' caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>		<StructureSection load='1o93' size='340' side='right' caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O93 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O93 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://pdbe.org/1o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1o93" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Methionine adenosyltransferase]]		[[Category: Methionine adenosyltransferase]]
-	[[Category: Rattus norvegicus]]
	[[Category: Gonzalez, B]]		[[Category: Gonzalez, B]]
	[[Category: Hermoso, J A]]		[[Category: Hermoso, J A]]

OCA at 23:56, 24 December 2014

2014-12-24T23:56:25Z

←Older revision		Revision as of 23:56, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O93 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O93 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/METK1_RAT METK1_RAT]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Methionine adenosyltransferase]]		[[Category: Methionine adenosyltransferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Gonzalez, B.]]	+	[[Category: Gonzalez, B]]
-	[[Category: Hermoso, J A.]]	+	[[Category: Hermoso, J A]]
-	[[Category: Pajares, M A.]]	+	[[Category: Pajares, M A]]
-	[[Category: Sanz-Aparicio, J.]]	+	[[Category: Sanz-Aparicio, J]]
	[[Category: Adenosyltransferase]]		[[Category: Adenosyltransferase]]
	[[Category: Methionine and atp binding]]		[[Category: Methionine and atp binding]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 14:49, 28 September 2014

2014-09-28T14:49:42Z

←Older revision		Revision as of 14:49, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1o93.~~png~~\|~~left~~\|200px]]	+	==METHIONINE ADENOSYLTRANSFERASE COMPLEXED WITH ATP AND A L-METHIONINE ANALOGOUS==
		+	<StructureSection load='1o93' size='340' side='right' caption='[[1o93]], [[Resolution\|resolution]] 3.49Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1o93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O93 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LIS:(2S,4S)-2-AMINO-4,5-EPOXIPENTANOIC+ACID'>LIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o90\|1o90]], [[1o92\|1o92]], [[1qm4\|1qm4]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=1o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o93 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o93 RCSB], [http://www.ebi.ac.uk/pdbsum/1o93 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o9/1o93_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Methionine adenosyltransferases (MATs) are a family of enzymes in charge of synthesising S-adenosylmethionine (SAM), the most important methyl donor present in living organisms. These enzymes use methionine and ATP as reaction substrates, which react in a S(N)2 fashion where the sulphur atom from methionine attacks C5' from ATP while triphosphate chain is cleaved. A MAT liver specific isoenzyme has been detected, which exists in two distinct oligomeric forms, a dimer (MAT III) and a tetramer (MAT I). Our previously reported crystal structure of MAT I complexed with an inhibitor led to the identification of the methionine-binding site. We present here the results obtained from the complex of MAT I with a competitive inhibitor of methionine, (2S,4S)-amino-4,5-epoxypentanoic acid (AEP), which presents the same features at the methionine binding site reported before. We have also analysed several complexes of this enzyme with methionine and ATP and analogues of them, in order to characterise the interaction that is produced between both substrates. The crystal structures of the complexes reveal how the substrates recognise each other at the active site of the enzyme, and suggest a putative binding site for the product SAM. The residues involved in the interactions of substrates and products with MAT have been identified, and the results agree with all the previous data concerning mutagenesis experiments and crystallographic work. Moreover, all the information provided from the analysis of the complexes has allowed us to postulate a catalytic mechanism for this family of enzymes. In particular, we propose a key role for Lys182 in the correct positioning of the substrates, and Asp135(*), in stabilising the sulphonium group formed in the product (SAM).

-	~~{{STRUCTURE_1o93\| PDB=1o93 \| SCENE= }}~~	+	Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism.,Gonzalez B, Pajares MA, Hermoso JA, Guillerm D, Guillerm G, Sanz-Aparicio J J Mol Biol. 2003 Aug 8;331(2):407-16. PMID:12888348<ref>PMID:12888348</ref>

-	~~===METHIONINE ADENOSYLTRANSFERASE COMPLEXED WITH ATP AND A L-METHIONINE ANALOGOUS===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12888348}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1o93]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA].~~	+

	==See Also==		==See Also==
-	*[[~~S-adenosylmethionine~~ synthetase\|~~S-adenosylmethionine~~ synthetase]]	+	*[[SAM synthetase\|SAM synthetase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:012888348<~~/~~ref~~><~~ref group="xtra">PMID:010873471</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Methionine adenosyltransferase]]		[[Category: Methionine adenosyltransferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]

OCA at 10:26, 20 October 2012

2012-10-20T10:26:03Z

←Older revision		Revision as of 10:26, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1o93]] is a 2 chain structure ~~of [[S-adenosylmethionine synthetase]]~~ with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA].	+	[[1o93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O93 OCA].

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