2dab - Revision history

OCA at 06:43, 9 August 2023

2023-08-09T06:43:02Z

← Older revision		Revision as of 06:43, 9 August 2023
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	<StructureSection load='2dab' size='340' side='right'caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2dab' size='340' side='right'caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bacym Bacym~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._YM-1 Bacillus sp. YM-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DAB 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>~~</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='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks'>[https~~:~~//en.wikipedia.org/wiki/D~~-~~amino~~-~~acid_transaminase D-amino-acid transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21]~~ </~~span~~></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></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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [https://pdbe.org/2dab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [https://www.ebi.ac.uk/pdbsum/2dab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dab 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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [https://pdbe.org/2dab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [https://www.ebi.ac.uk/pdbsum/2dab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dab ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/DAAA_BACYM DAAA_BACYM]] Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.<ref>PMID:2914916</ref> <ref>PMID:9538014</ref>		[https://www.uniprot.org/uniprot/DAAA_BACYM DAAA_BACYM] Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.<ref>PMID:2914916</ref> <ref>PMID:9538014</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacym]]~~		[[Category: Bacillus sp. YM-1]]
	~~[[Category: D~~-~~amino-acid transaminase~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Esaki, N]]		[[Category: Esaki N]]
	[[Category: Kashima, A]]		[[Category: Kashima A]]
	[[Category: Kishimoto, K]]		[[Category: Kishimoto K]]
	[[Category: Peisach, D]]		[[Category: Peisach D]]
	[[Category: Petsko~~, G A~~]]		[[Category: Petsko GA]]
	[[Category: Ringe, D]]		[[Category: Ringe D]]
	[[Category: Sugio, S]]		[[Category: Sugio S]]
	[[Category: Yoshimura, T]]		[[Category: Yoshimura T]]
	~~[[Category: Alpha-ketoglutamic acid]]~~
	~~[[Category: Aminotransferase]]~~
	~~[[Category: D-alanine]]~~
	~~[[Category: D-amino acid]]~~
	~~[[Category: Pyridoxal-5'-phosphate]]~~
	~~[[Category: Transferase~~]]

OCA at 15:40, 3 November 2021

2021-11-03T15:40:44Z

← Older revision		Revision as of 15:40, 3 November 2021
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	<StructureSection load='2dab' size='340' side='right'caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2dab' size='340' side='right'caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bacym Bacym]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2DAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacym Bacym]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DAB 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></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></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [~~http~~://pdbe.org/2dab PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2dab PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2dab 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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [https://pdbe.org/2dab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [https://www.ebi.ac.uk/pdbsum/2dab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dab ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/DAAA_BACYM DAAA_BACYM]] Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.<ref>PMID:2914916</ref> <ref>PMID:9538014</ref>		[[https://www.uniprot.org/uniprot/DAAA_BACYM DAAA_BACYM]] Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.<ref>PMID:2914916</ref> <ref>PMID:9538014</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:48, 4 March 2020

2020-03-04T07:48:18Z

← Older revision		Revision as of 07:48, 4 March 2020
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	==L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE==		==L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE==
	<StructureSection load='2dab' size='340' side='right' caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2dab' size='340' side='right'caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacym Bacym]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacym Bacym]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DAB FirstGlance]. <br>
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	==See Also==		==See Also==
	*[[Aminotransferase\|Aminotransferase]]		*[[Aminotransferase 3D structures\|Aminotransferase 3D structures]]
	*[[Aspartate ~~Aminotransferase~~\|Aspartate ~~Aminotransferase~~]]		*[[Aspartate aminotransferase 3D structures\|Aspartate aminotransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Bacym]]		[[Category: Bacym]]
	[[Category: D-amino-acid transaminase]]		[[Category: D-amino-acid transaminase]]
			[[Category: Large Structures]]
	[[Category: Esaki, N]]		[[Category: Esaki, N]]
	[[Category: Kashima, A]]		[[Category: Kashima, A]]

OCA at 06:36, 30 May 2018

2018-05-30T06:36:07Z

← Older revision		Revision as of 06:36, 30 May 2018
Line 1:		Line 1:

	==L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE==		==L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE==
	<StructureSection load='2dab' size='340' side='right' caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2dab' size='340' side='right' caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>
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	</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></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></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [http://pdbe.org/2dab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [http://www.ebi.ac.uk/pdbsum/2dab 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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [http://pdbe.org/2dab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [http://www.ebi.ac.uk/pdbsum/2dab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dab ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/da/2dab_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/da/2dab_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>
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	==See Also==		==See Also==
	*[[Aminotransferase\|Aminotransferase]]		*[[Aminotransferase\|Aminotransferase]]
			*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:23, 8 February 2016

2016-02-08T20:23:10Z

← Older revision		Revision as of 20:23, 8 February 2016
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	<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=2dab ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	==See Also==		==See Also==
	*[[~~Aspartate~~ Aminotransferase\|~~Aspartate~~ Aminotransferase]]		*[[Aminotransferase\|Aminotransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:04, 10 September 2015

2015-09-10T15:04:48Z

← Older revision		Revision as of 15:04, 10 September 2015
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	<StructureSection load='2dab' size='340' side='right' caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2dab' size='340' side='right' caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_sp. Bacillus sp.~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacym Bacym]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DAB 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></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></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [http://www.ebi.ac.uk/pdbsum/2dab 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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [http://pdbe.org/2dab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [http://www.ebi.ac.uk/pdbsum/2dab PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2dab" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus sp~~]]		[[Category: Bacym]]
	[[Category: D-amino-acid transaminase]]		[[Category: D-amino-acid transaminase]]
	[[Category: Esaki, N]]		[[Category: Esaki, N]]

OCA at 01:55, 25 December 2014

2014-12-25T01:55:13Z

← Older revision		Revision as of 01:55, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DAB FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><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></td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [http://www.ebi.ac.uk/pdbsum/2dab 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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [http://www.ebi.ac.uk/pdbsum/2dab PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/DAAA_BACYM DAAA_BACYM]] Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.<ref>PMID:2914916</ref> <ref>PMID:9538014</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Bacillus sp.]]		[[Category: Bacillus sp]]
	[[Category: D-amino-acid transaminase]]		[[Category: D-amino-acid transaminase]]
	[[Category: Esaki, N.]]		[[Category: Esaki, N]]
	[[Category: Kashima, A.]]		[[Category: Kashima, A]]
	[[Category: Kishimoto, K.]]		[[Category: Kishimoto, K]]
	[[Category: Peisach, D.]]		[[Category: Peisach, D]]
	[[Category: Petsko, G A.]]		[[Category: Petsko, G A]]
	[[Category: Ringe, D.]]		[[Category: Ringe, D]]
	[[Category: Sugio, S.]]		[[Category: Sugio, S]]
	[[Category: Yoshimura, T.]]		[[Category: Yoshimura, T]]
	[[Category: Alpha-ketoglutamic acid]]		[[Category: Alpha-ketoglutamic acid]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]

OCA at 05:47, 29 September 2014

2014-09-29T05:47:28Z

← Older revision		Revision as of 05:47, 29 September 2014
Line 1:		Line 1:
	[[Image:~~2dab~~.~~png~~\|~~left~~\|~~200px~~]]		==L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE==
			<StructureSection load='2dab' size='340' side='right' caption='[[2dab]], [[Resolution\|resolution]] 2.00Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2dab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DAB FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] </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=2dab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dab RCSB], [http://www.ebi.ac.uk/pdbsum/2dab 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/da/2dab_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 ==
			The leucine-to-alanine mutation at residue 201 of D-amino acid aminotransferase provides a unique enzyme which gradually loses its activity while catalyzing the normal transamination; the co-enzyme form is converted from pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate upon the inactivation [Kishimoto,K., Yoshimura,T., Esaki,N., Sugio,S., Manning,J.M. and Soda,K. (1995) J. Biochem., 117, 691-696]. Crystal structures of both co-enzyme forms of the mutant enzyme have been determined at 2.0 A resolution: they are virtually identical, and are quite similar to that of the wild-type enzyme. Significant differences in both forms of the mutant are localized only on the bound co-enzyme, the side chains of Lys145 and Tyr31, and a water molecule sitting on the putative substrate binding site. Detailed comparisons of the structures of the mutant, together with that of the pyridoxamine-5'-phosphate form of the wild-type enzyme, imply that Leu201 would play a crucial role in the transamination reaction by keeping the pyridoxyl ring in the proper location without disturbing its oscillating motion, although the residue seems to not be especially important for the structural integrity of the enzyme.

	~~{{STRUCTURE_2dab\| PDB=2dab \| SCENE= }}~~		Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.,Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N Protein Eng. 1998 Aug;11(8):613-9. PMID:9749913<ref>PMID:9749913</ref>

	~~===L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_9749913}}~~

	~~==About this Structure==~~
	~~[[2dab]] is~~ a ~~2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp~~. ~~Bacillus sp~~.]. ~~Full crystallographic information is available from [http://oca.weizmann.ac.il~~/~~oca-bin/ocashort?id=2DAB OCA].~~

	==See Also==		==See Also==
	*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]		*[[Aspartate Aminotransferase\|Aspartate Aminotransferase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:009749913<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Bacillus sp.]]		[[Category: Bacillus sp.]]
	[[Category: D-amino-acid transaminase]]		[[Category: D-amino-acid transaminase]]

OCA at 11:21, 20 October 2012

2012-10-20T11:21:56Z

← Older revision		Revision as of 11:21, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[2dab]] is a 2 chain structure ~~of [[Aspartate Aminotransferase]]~~ with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA].		[[2dab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA].

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

OCA: Protected "2dab" [edit=sysop:move=sysop]

2012-07-26T05:07:25Z

Protected "2dab" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:07, 26 July 2012
(No difference)