5bj4 - Revision history

OCA at 18:05, 20 September 2023

OCA — Wed, 20 Sep 2023 18:05:09 GMT

←Older revision		Revision as of 18:05, 20 September 2023
Line 3:		Line 3:
	<StructureSection load='5bj4' size='340' side='right'caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5bj4' size='340' side='right'caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Thet8 Thet8~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PLP:PYRIDOXAL~~-~~5-PHOSPHATE'>PLP</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]] 2Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1b5p\|1b5p]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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/Aspartate_transaminase Aspartate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1]~~ </~~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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [https://pdbe.org/5bj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [https://www.ebi.ac.uk/pdbsum/5bj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bj4 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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [https://pdbe.org/5bj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [https://www.ebi.ac.uk/pdbsum/5bj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bj4 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/AAPAT_THET8 AAPAT_THET8] Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).<ref>PMID:25070637</ref> <ref>PMID:30771275</ref> <ref>PMID:8907187</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Aspartate transaminase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Thet8~~]]	+	[[Category: Thermus thermophilus HB8]]
-	[[Category: Hirotsu, K]]	+	[[Category: Hirotsu K]]
-	[[Category: Kawaguchi~~, S I~~]]	+	[[Category: Kawaguchi SI]]
-	[[Category: Kuramitsu, S]]	+	[[Category: Kuramitsu S]]
-	[[Category: Miyahara, I]]	+	[[Category: Miyahara I]]
-	[[Category: Nakai, T]]	+	[[Category: Nakai T]]
-	[[Category: Ura, H]]	+	[[Category: Ura H]]
-	~~[[Category: Aminotransferase]]~~	+
-	~~[[Category: Pyridoxal enzyme]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 15:50, 3 November 2021

OCA — Wed, 03 Nov 2021 15:50:43 GMT

←Older revision		Revision as of 15:50, 3 November 2021
Line 3:		Line 3:
	<StructureSection load='5bj4' size='340' side='right'caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5bj4' size='340' side='right'caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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">[[1b5p\|1b5p]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b5p\|1b5p]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [~~http~~://pdbe.org/5bj4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5bj4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5bj4 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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [https://pdbe.org/5bj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [https://www.ebi.ac.uk/pdbsum/5bj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bj4 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 08:49, 11 March 2020

OCA — Wed, 11 Mar 2020 08:49:13 GMT

←Older revision		Revision as of 08:49, 11 March 2020
Line 1:		Line 1:
		+
	==THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2==		==THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2==
-	<StructureSection load='5bj4' size='340' side='right' caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5bj4' size='340' side='right'caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1b5p\|1b5p]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1b5p\|1b5p]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [http://pdbe.org/5bj4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [http://www.ebi.ac.uk/pdbsum/5bj4 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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [http://pdbe.org/5bj4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [http://www.ebi.ac.uk/pdbsum/5bj4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bj4 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/5bj4_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/5bj4_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:

	==See Also==		==See Also==
-	*[[Aspartate ~~Aminotransferase~~\|Aspartate ~~Aminotransferase~~]]	+	*[[Aspartate aminotransferase 3D structures\|Aspartate aminotransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
		+	[[Category: Large Structures]]
	[[Category: Thet8]]		[[Category: Thet8]]
	[[Category: Hirotsu, K]]		[[Category: Hirotsu, K]]

OCA at 10:48, 9 February 2016

OCA — Tue, 09 Feb 2016 10:48:32 GMT

←Older revision		Revision as of 10:48, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='5bj4' size='340' side='right' caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5bj4' size='340' side='right' caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermus_thermophilus Thermus thermophilus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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">[[1b5p\|1b5p]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1b5p\|1b5p]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [http://www.ebi.ac.uk/pdbsum/5bj4 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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [http://pdbe.org/5bj4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [http://www.ebi.ac.uk/pdbsum/5bj4 PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 16:		Line 16:
	<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=5bj4 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 26:		Line 26:
	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 5bj4" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
-	[[Category: ~~Thermus thermophilus~~]]	+	[[Category: Thet8]]
	[[Category: Hirotsu, K]]		[[Category: Hirotsu, K]]
	[[Category: Kawaguchi, S I]]		[[Category: Kawaguchi, S I]]

OCA at 16:53, 10 December 2014

OCA — Wed, 10 Dec 2014 16:53:17 GMT

←Older revision		Revision as of 16:53, 10 December 2014
Line 1:		Line 1:
-	[[~~Image:~~5bj4.~~png~~\|~~left~~\|200px]]	+	==THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2==
		+	<StructureSection load='5bj4' size='340' side='right' caption='[[5bj4]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5bj4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BJ4 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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">[[1b5p\|1b5p]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=5bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bj4 RCSB], [http://www.ebi.ac.uk/pdbsum/5bj4 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/bj/5bj4_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 ==
		+	Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic substrates. During the course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently. The introduction of a mobile Arg292* residue into ttAspAT was the key step in the change to a "dual-substrate" enzyme. The substrate recognition mechanism of this thermostable "dual-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.

-	~~{{STRUCTURE_5bj4\| PDB=5bj4 \| SCENE= }}~~	+	Substrate recognition mechanism of thermophilic dual-substrate enzyme.,Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S J Biochem. 2001 Jul;130(1):89-98. PMID:11432784<ref>PMID:11432784</ref>

-	~~===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11432784}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[5bj4]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Thermus_thermophilus Thermus thermophilus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA].~~	+

	==See Also==		==See Also==
	*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]		*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:011432784<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
-	[[Category: Hirotsu, K.]]	+	[[Category: Hirotsu, K]]
-	[[Category: Kawaguchi, S I.]]	+	[[Category: Kawaguchi, S I]]
-	[[Category: Kuramitsu, S.]]	+	[[Category: Kuramitsu, S]]
-	[[Category: Miyahara, I.]]	+	[[Category: Miyahara, I]]
-	[[Category: Nakai, T.]]	+	[[Category: Nakai, T]]
-	[[Category: Ura, H.]]	+	[[Category: Ura, H]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]
	[[Category: Pyridoxal enzyme]]		[[Category: Pyridoxal enzyme]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 13:37, 20 October 2012

OCA — Sat, 20 Oct 2012 13:37:57 GMT

←Older revision		Revision as of 13:37, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[5bj4]] is a 2 chain structure ~~of [[Aspartate Aminotransferase]]~~ with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA].	+	[[5bj4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA].

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

OCA: Protected "5bj4" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 12:35:19 GMT

Protected "5bj4" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:35, 26 July 2012

OCA at 12:35, 26 July 2012

OCA — Thu, 26 Jul 2012 12:35:17 GMT

←Older revision		Revision as of 12:35, 26 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:5bj4.png\|left\|200px]]		[[Image:5bj4.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_5bj4", 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_5bj4\| PDB=5bj4 \| SCENE= }}		{{STRUCTURE_5bj4\| PDB=5bj4 \| SCENE= }}

	===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2===		===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_11432784}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 11432784 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_11432784}}		{{ABSTRACT_PUBMED_11432784}}

	==About this Structure==		==About this Structure==
-	~~5BJ4~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA].	+	[[5bj4]] is a 2 chain structure of [[Aspartate Aminotransferase]] with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA].
		+
		+	==See Also==
		+	*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11432784~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011432784</ref><references group="xtra"/>
	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
Line 34:		Line 25:
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]
	[[Category: Pyridoxal enzyme]]		[[Category: Pyridoxal enzyme]]
-		+	[[Category: Transferase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 09:16:00 2009''~~	+

OCA at 07:16, 17 February 2009

OCA — Tue, 17 Feb 2009 07:16:01 GMT

←Older revision		Revision as of 07:16, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	5BJ4 is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA].	+	5BJ4 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ4 OCA].

	==Reference==		==Reference==
-	~~Substrate recognition mechanism of thermophilic dual-substrate enzyme., Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S, J Biochem. 2001 Jul;130(1):89-98.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/11432784 11432784]~~	+	<ref group="xtra">PMID:11432784</ref><references group="xtra"/>
	[[Category: Aspartate transaminase]]		[[Category: Aspartate transaminase]]
-	[[Category: Single protein]]
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
	[[Category: Hirotsu, K.]]		[[Category: Hirotsu, K.]]
Line 36:		Line 35:
	[[Category: Pyridoxal enzyme]]		[[Category: Pyridoxal enzyme]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Jul 3 13~~:57:~~10 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:16:00 2009''

OCA at 10:57, 3 July 2008

OCA — Thu, 03 Jul 2008 10:57:11 GMT

←Older revision		Revision as of 10:57, 3 July 2008
Line 1:		Line 1:
-	[[Image:5bj4.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:5bj4.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_5bj4\| PDB=5bj4 \| SCENE= }}		{{STRUCTURE_5bj4\| PDB=5bj4 \| SCENE= }}

-	~~'''~~THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2~~'''~~	+	===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2===


-	~~==Overview==~~	+	<!--
-	~~Aspartate aminotransferase from an extremely thermophilic bacterium~~, ~~Thermus thermophilus HB8 (ttAspAT)~~, ~~has been believed~~ to ~~be specific for an acidic substrate. However, stepwise introduction of mutations in~~ the ~~active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme~~. ~~The final mutant, [S15D, T17V, K109S, S292R] ttAspAT~~, is ~~active toward both acidic and hydrophobic substrates. During~~ the ~~course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently~~. ~~The introduction of a mobile Arg292* residue into ttAspAT was the key step in the change to a "dual~~-~~substrate" enzyme. The substrate recognition mechanism of this thermostable "dual~~-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.	+	The line below this paragraph, {{ABSTRACT_PUBMED_11432784}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 11432784 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_11432784}}

	==About this Structure==		==About this Structure==
Line 31:		Line 35:
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]
	[[Category: Pyridoxal enzyme]]		[[Category: Pyridoxal enzyme]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:32:11 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:57:10 2008''