2vvm - Revision history

OCA at 07:08, 1 May 2024

2024-05-01T07:08:58Z

← Older revision		Revision as of 07:08, 1 May 2024
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	<StructureSection load='2vvm' size='340' side='right'caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vvm' size='340' side='right'caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~A._niger A.~~ niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VVM FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=EDO:1,2~~-~~ETHANEDIOL'>EDO</scene>~~, ~~<scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.85Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2vvl\|2vvl]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4]~~ </~~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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [https://pdbe.org/2vvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [https://www.ebi.ac.uk/pdbsum/2vvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vvm 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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [https://pdbe.org/2vvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [https://www.ebi.ac.uk/pdbsum/2vvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vvm ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/AOFN_ASPNG AOFN_ASPNG]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=2vvm 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=2vvm ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Monoamine oxidase from Aspergillus niger (MAO-N) is a flavoenzyme that catalyses the oxidative deamination of primary amines. MAO-N has been used as the starting model for a series of directed evolution experiments, resulting in mutants of improved activity and broader substrate specificity, suitable for application in the preparative deracemisation of primary, secondary and tertiary amines when used as part of a chemoenzymatic oxidation-reduction cycle. The structures of a three-point mutant (Asn336Ser/Met348Lys/Ile246Met or MAO-N-D3) and a five-point mutant (Asn336Ser/Met348Lys/Ile246Met/Thr384Asn/Asp385Ser or MAO-N-D5) have been obtained using a multiple-wavelength anomalous diffraction experiment on a selenomethionine derivative of the truncated MAO-N-D5 enzyme. MAO-N exists as a homotetramer with a large channel at its centre and shares some structural features with human MAO B (MAO-B). A hydrophobic cavity extends from the protein surface to the active site, where a non-covalently bound flavin adenine dinucleotide (FAD) sits at the base of an 'aromatic cage,' the sides of which are formed by Trp430 and Phe466. A molecule of l-proline was observed near the FAD, and this ligand superimposed well with isatin, a reversible inhibitor of MAO-B, when the structures of MAO-N proline and MAO-B-isatin were overlaid. Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site. The two additional mutations, Thr384Asn and Asp385Ser, that occur in the MAO-N-D5 variant, which is able to oxidise tertiary amines, appear to influence the active-site environment remotely through changes in tertiary structure that perturb the side chain of Phe382, again altering the steric and electronic character of the active site near FAD. The possible implications of the change in steric and electronic environment caused by relevant mutations are discussed with respect to the improved catalytic efficiency of the MAO-N variants described in the literature.

	The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution.,Atkin KE, Reiss R, Koehler V, Bailey KR, Hart S, Turkenburg JP, Turner NJ, Brzozowski AM, Grogan G J Mol Biol. 2008 Dec 31;384(5):1218-31. Epub 2008 Oct 14. PMID:18951902<ref>PMID:18951902</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2vvm" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Monoamine oxidase\|Monoamine oxidase]]		*[[Monoamine oxidase\|Monoamine oxidase]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: A. niger]]		[[Category: Aspergillus niger]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Monoamine oxidase]]~~		[[Category: Atkin KE]]
	[[Category: Atkin~~, K E~~]]		[[Category: Brzozowski AM]]
	[[Category: Brzozowski~~, A M~~]]		[[Category: Grogan GJ]]
	[[Category: Grogan~~, G J~~]]		[[Category: Hart S]]
	[[Category: Hart, S]]		[[Category: Turkenburg JP]]
	[[Category: Turkenburg~~, J P]]~~
	~~[[Category: Aspergillus niger]]~~
	~~[[Category: Directed evolution variant]]~~
	~~[[Category: Enantioselectivity]]~~
	~~[[Category: Fad]]~~
	~~[[Category: Flavoprotein]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Peroxisome~~]]

OCA at 11:47, 30 March 2022

2022-03-30T11:47:04Z

← Older revision		Revision as of 11:47, 30 March 2022
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	<StructureSection load='2vvm' size='340' side='right'caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vvm' size='340' side='right'caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2VVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VVM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vvl\|2vvl]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [~~http~~://pdbe.org/2vvm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vvm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vvm 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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [https://pdbe.org/2vvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [https://www.ebi.ac.uk/pdbsum/2vvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vvm ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 08:34, 25 June 2020

2020-06-25T08:34:41Z

← Older revision		Revision as of 08:34, 25 June 2020
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	==The structure of MAO-N-D5, a variant of monoamine oxidase from Aspergillus niger.==		==The structure of MAO-N-D5, a variant of monoamine oxidase from Aspergillus niger.==
	<StructureSection load='2vvm' size='340' side='right' caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vvm' size='340' side='right'caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VVM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://pdbe.org/2vvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vvm 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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://pdbe.org/2vvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vvm ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	</StructureSection>		</StructureSection>
	[[Category: A. niger]]		[[Category: A. niger]]
			[[Category: Large Structures]]
	[[Category: Monoamine oxidase]]		[[Category: Monoamine oxidase]]
	[[Category: Atkin, K E]]		[[Category: Atkin, K E]]

OCA at 21:00, 19 September 2018

2018-09-19T21:00:10Z

← Older revision		Revision as of 21:00, 19 September 2018
Line 1:		Line 1:
	==~~THE STRUCTURE OF~~ MAO-N-D5, ~~A VARIANT OF MONOAMINE OXIDASE FROM ASPERGILLUS NIGER~~.==
			==The structure of MAO-N-D5, a variant of monoamine oxidase from Aspergillus niger.==
	<StructureSection load='2vvm' size='340' side='right' caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vvm' size='340' side='right' caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://pdbe.org/2vvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm 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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://pdbe.org/2vvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vvm 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/vv/2vvm_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vv/2vvm_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>

OCA at 08:01, 9 February 2016

2016-02-09T08:01:07Z

← Older revision		Revision as of 08:01, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='2vvm' size='340' side='right' caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vvm' size='340' side='right' caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Aspergillus_niger Aspergillus~~ niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VVM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm 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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://pdbe.org/2vvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm 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=2vvm 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 2vvm" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Aspergillus~~ niger]]		[[Category: A. niger]]
	[[Category: Monoamine oxidase]]		[[Category: Monoamine oxidase]]
	[[Category: Atkin, K E]]		[[Category: Atkin, K E]]
Line 40:		Line 41:
	[[Category: Hart, S]]		[[Category: Hart, S]]
	[[Category: Turkenburg, J P]]		[[Category: Turkenburg, J P]]
			[[Category: Aspergillus niger]]
	[[Category: Directed evolution variant]]		[[Category: Directed evolution variant]]
	[[Category: Enantioselectivity]]		[[Category: Enantioselectivity]]

OCA at 15:37, 19 January 2015

2015-01-19T15:37:37Z

← Older revision		Revision as of 15:37, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VVM FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm 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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm PDBsum]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Aspergillus niger]]		[[Category: Aspergillus niger]]
	[[Category: Monoamine oxidase]]		[[Category: Monoamine oxidase]]
	[[Category: Atkin, K E.]]		[[Category: Atkin, K E]]
	[[Category: Brzozowski, A M.]]		[[Category: Brzozowski, A M]]
	[[Category: Grogan, G J.]]		[[Category: Grogan, G J]]
	[[Category: Hart, S.]]		[[Category: Hart, S]]
	[[Category: Turkenburg, J P~~.]]~~		[[Category: Turkenburg, J P]]
	~~[[Category: Aspergillus niger~~]]
	[[Category: Directed evolution variant]]		[[Category: Directed evolution variant]]
	[[Category: Enantioselectivity]]		[[Category: Enantioselectivity]]
	[[Category: Fad]]		[[Category: Fad]]
	[[Category: Flavoprotein]]		[[Category: Flavoprotein]]
	~~[[Category: Monoamine oxidase]]~~
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Peroxisome]]		[[Category: Peroxisome]]

OCA at 07:50, 29 September 2014

2014-09-29T07:50:03Z

← Older revision		Revision as of 07:50, 29 September 2014
Line 1:		Line 1:
	[[Image:~~2vvm~~.~~png~~\|~~left~~\|~~200px~~]]		==THE STRUCTURE OF MAO-N-D5, A VARIANT OF MONOAMINE OXIDASE FROM ASPERGILLUS NIGER.==
			<StructureSection load='2vvm' size='340' side='right' caption='[[2vvm]], [[Resolution\|resolution]] 1.85Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VVM FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vvl\|2vvl]]</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vvm RCSB], [http://www.ebi.ac.uk/pdbsum/2vvm 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/vv/2vvm_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 ==
			Monoamine oxidase from Aspergillus niger (MAO-N) is a flavoenzyme that catalyses the oxidative deamination of primary amines. MAO-N has been used as the starting model for a series of directed evolution experiments, resulting in mutants of improved activity and broader substrate specificity, suitable for application in the preparative deracemisation of primary, secondary and tertiary amines when used as part of a chemoenzymatic oxidation-reduction cycle. The structures of a three-point mutant (Asn336Ser/Met348Lys/Ile246Met or MAO-N-D3) and a five-point mutant (Asn336Ser/Met348Lys/Ile246Met/Thr384Asn/Asp385Ser or MAO-N-D5) have been obtained using a multiple-wavelength anomalous diffraction experiment on a selenomethionine derivative of the truncated MAO-N-D5 enzyme. MAO-N exists as a homotetramer with a large channel at its centre and shares some structural features with human MAO B (MAO-B). A hydrophobic cavity extends from the protein surface to the active site, where a non-covalently bound flavin adenine dinucleotide (FAD) sits at the base of an 'aromatic cage,' the sides of which are formed by Trp430 and Phe466. A molecule of l-proline was observed near the FAD, and this ligand superimposed well with isatin, a reversible inhibitor of MAO-B, when the structures of MAO-N proline and MAO-B-isatin were overlaid. Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site. The two additional mutations, Thr384Asn and Asp385Ser, that occur in the MAO-N-D5 variant, which is able to oxidise tertiary amines, appear to influence the active-site environment remotely through changes in tertiary structure that perturb the side chain of Phe382, again altering the steric and electronic character of the active site near FAD. The possible implications of the change in steric and electronic environment caused by relevant mutations are discussed with respect to the improved catalytic efficiency of the MAO-N variants described in the literature.

	~~{{STRUCTURE_2vvm\| PDB=2vvm \| SCENE= }}~~		The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution.,Atkin KE, Reiss R, Koehler V, Bailey KR, Hart S, Turkenburg JP, Turner NJ, Brzozowski AM, Grogan G J Mol Biol. 2008 Dec 31;384(5):1218-31. Epub 2008 Oct 14. PMID:18951902<ref>PMID:18951902</ref>

	~~===THE STRUCTURE OF MAO-N-D5~~, ~~A VARIANT OF MONOAMINE OXIDASE FROM ASPERGILLUS NIGER.===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_18951902}}~~

	~~==About this Structure==~~
	~~[[2vvm]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Aspergillus_niger Aspergillus niger]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA].~~

	==See Also==		==See Also==
	*[[Monoamine oxidase\|Monoamine oxidase]]		*[[Monoamine oxidase\|Monoamine oxidase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:018951902<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Aspergillus niger]]		[[Category: Aspergillus niger]]
	[[Category: Monoamine oxidase]]		[[Category: Monoamine oxidase]]

OCA at 13:12, 20 October 2012

2012-10-20T13:12:35Z

← Older revision		Revision as of 13:12, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[2vvm]] is a 2 chain structure ~~of [[Monoamine oxidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA].		[[2vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA].

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

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

2012-07-26T11:14:35Z

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

← Older revision	Revision as of 11:14, 26 July 2012
(No difference)

OCA at 11:14, 26 July 2012

2012-07-26T11:14:34Z

← Older revision		Revision as of 11:14, 26 July 2012
Line 1:		Line 1:
	~~{{Seed}}~~
	[[Image:2vvm.png\|left\|200px]]		[[Image:2vvm.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2vvm", 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_2vvm\| PDB=2vvm \| SCENE= }}		{{STRUCTURE_2vvm\| PDB=2vvm \| SCENE= }}

	===THE STRUCTURE OF MAO-N-D5, A VARIANT OF MONOAMINE OXIDASE FROM ASPERGILLUS NIGER.===		===THE STRUCTURE OF MAO-N-D5, A VARIANT OF MONOAMINE OXIDASE FROM ASPERGILLUS NIGER.===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_18951902}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 18951902 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_18951902}}		{{ABSTRACT_PUBMED_18951902}}

	==About this Structure==		==About this Structure==
	~~2VVM~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA].		[[2vvm]] is a 2 chain structure of [[Monoamine oxidase]] with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVM OCA].

			==See Also==
			*[[Monoamine oxidase\|Monoamine oxidase]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~18951902~~</ref><references group="xtra"/>		<ref group="xtra">PMID:018951902</ref><references group="xtra"/>
	[[Category: Aspergillus niger]]		[[Category: Aspergillus niger]]
			[[Category: Monoamine oxidase]]
	[[Category: Atkin, K E.]]		[[Category: Atkin, K E.]]
	[[Category: Brzozowski, A M.]]		[[Category: Brzozowski, A M.]]
Line 38:		Line 30:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Peroxisome]]		[[Category: Peroxisome]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:11:19 2009''~~