4ec3 - Revision history

OCA at 14:57, 14 March 2024

OCA — Thu, 14 Mar 2024 14:57:40 GMT

←Older revision		Revision as of 14:57, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</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]] 2.6501Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [https://pdbe.org/4ec3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ec3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ec3 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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [https://pdbe.org/4ec3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ec3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ec3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/RETO_ESCCA RETO_ESCCA]] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.	+	[https://www.uniprot.org/uniprot/RETO_ESCCA RETO_ESCCA] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Berberine bridge enzyme (BBE) is a paradigm for the class of bicovalently flavinylated oxidases, which catalyzes the oxidative cyclization of (S)-reticuline to (S)-scoulerine. His174 was identified as a potentially important active site residue because its putative role for the stabilization of the reduced state of the flavin cofactor. It is also strictly conserved in the family of BBE-like oxidases. Here, we present a detailed biochemical and structural characterization of the BBE His174Ala variant supporting its role for catalysis as well as structural organization of the active site. Substantial changes in all kinetic parameters and a decrease in midpoint potential were observed for the BBE His174Ala variant protein. Moreover, the crystal structure of the BBE His174Ala showed significant structural rearrangements compared to wild type enzyme. Based on our findings, we propose that His174 is part of a hydrogen bonding network that stabilizes the negative charge at the N(1)-C(2)=O locus via interaction with the hydroxyl group at the C2' of the ribityl side chain. Hence replacement of this residue with alanine abolishes the stabilizing effect and results in drastically decreased kinetic parameters as well as a lower midpoint redox potential.	+
-		+
-	Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme.,Wallner S, Winkler A, Riedl S, Dully C, Horvath S, Gruber K, Macheroux P Biochemistry. 2012 Jul 3. PMID:22757961<ref>PMID:22757961</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4ec3" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Reticuline oxidase\|Reticuline oxidase]]		*[[Reticuline oxidase\|Reticuline oxidase]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:03, 28 September 2022

OCA — Wed, 28 Sep 2022 07:03:58 GMT

←Older revision		Revision as of 07:03, 28 September 2022
Line 1:		Line 1:

	==Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline==		==Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline==
-	<StructureSection load='4ec3' size='340' side='right' caption='[[4ec3]], [[Resolution\|resolution]] 2.65Å' scene=''>	+	<StructureSection load='4ec3' size='340' side='right'caption='[[4ec3]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~California_poppy California poppy~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=~~NAG~~:~~N-ACETYL~~-D-~~GLUCOSAMINE~~'>~~NAG~~</scene>, <scene name='pdbligand=~~REN~~:~~(S)~~-~~RETICULINE~~'>~~REN~~</scene>, <scene name='pdbligand=~~MAN~~:~~ALPHA~~-~~D-MANNOSE~~'>~~MAN~~</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2j\|3d2j]], [[3d2d\|3d2d]], [[3fw7\|3fw7]], [[3fw8\|3fw8]]</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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [https://pdbe.org/4ec3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ec3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ec3 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBE, BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 California poppy])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [~~http~~://pdbe.org/4ec3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ec3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ec3 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RETO_ESCCA RETO_ESCCA]] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.	+	[[https://www.uniprot.org/uniprot/RETO_ESCCA RETO_ESCCA]] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4ec3" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ec3" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Reticuline oxidase\|Reticuline oxidase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~California poppy~~]]	+	[[Category: Eschscholzia californica]]
-	[[Category: ~~Reticuline oxidase~~]]	+	[[Category: Large Structures]]
-	[[Category: Gruber, K]]	+	[[Category: Gruber K]]
-	[[Category: Macheroux, P]]	+	[[Category: Macheroux P]]
-	[[Category: Winkler, A]]	+	[[Category: Winkler A]]
-	~~[[Category: Bi-covalent flavinylation]]~~	+
-	~~[[Category: Fad]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: P-cresol methyl hydroxylase superfamily~~]]	+

OCA at 17:26, 5 August 2016

OCA — Fri, 05 Aug 2016 17:26:50 GMT

←Older revision		Revision as of 17:26, 5 August 2016
Line 1:		Line 1:
		+
	==Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline==		==Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline==
	<StructureSection load='4ec3' size='340' side='right' caption='[[4ec3]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='4ec3' size='340' side='right' caption='[[4ec3]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Eschscholzia_californica Eschscholzia californica~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/California_poppy California poppy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2j\|3d2j]], [[3d2d\|3d2d]], [[3fw7\|3fw7]], [[3fw8\|3fw8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2j\|3d2j]], [[3d2d\|3d2d]], [[3fw7\|3fw7]], [[3fw8\|3fw8]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBE, BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 ~~Eschscholzia californica~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBE, BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 California poppy])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ec3 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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [http://pdbe.org/4ec3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ec3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ec3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4ec3" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Eschscholzia californica~~]]	+	[[Category: California poppy]]
	[[Category: Reticuline oxidase]]		[[Category: Reticuline oxidase]]
	[[Category: Gruber, K]]		[[Category: Gruber, K]]

OCA at 04:25, 25 December 2014

OCA — Thu, 25 Dec 2014 04:25:15 GMT

←Older revision		Revision as of 04:25, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2j\|3d2j]], [[3d2d\|3d2d]], [[3fw7\|3fw7]], [[3fw8\|3fw8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2j\|3d2j]], [[3d2d\|3d2d]], [[3fw7\|3fw7]], [[3fw8\|3fw8]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBE, BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 Eschscholzia californica])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBE, BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 Eschscholzia californica])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ec3 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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ec3 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RETO_ESCCA RETO_ESCCA]] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 25:
	[[Category: Eschscholzia californica]]		[[Category: Eschscholzia californica]]
	[[Category: Reticuline oxidase]]		[[Category: Reticuline oxidase]]
-	[[Category: Gruber, K.]]	+	[[Category: Gruber, K]]
-	[[Category: Macheroux, P.]]	+	[[Category: Macheroux, P]]
-	[[Category: Winkler, A.]]	+	[[Category: Winkler, A]]
	[[Category: Bi-covalent flavinylation]]		[[Category: Bi-covalent flavinylation]]
	[[Category: Fad]]		[[Category: Fad]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: P-cresol methyl hydroxylase superfamily]]		[[Category: P-cresol methyl hydroxylase superfamily]]

OCA at 07:49, 9 July 2014

OCA — Wed, 09 Jul 2014 07:49:12 GMT

←Older revision		Revision as of 07:49, 9 July 2014
Line 1:		Line 1:
-	[[~~Image:~~4ec3.~~png~~\|~~left~~\|~~200px~~]]	+	==Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline==
		+	<StructureSection load='4ec3' size='340' side='right' caption='[[4ec3]], [[Resolution\|resolution]] 2.65Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EC3 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2j\|3d2j]], [[3d2d\|3d2d]], [[3fw7\|3fw7]], [[3fw8\|3fw8]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBE, BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 Eschscholzia californica])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ec3 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Berberine bridge enzyme (BBE) is a paradigm for the class of bicovalently flavinylated oxidases, which catalyzes the oxidative cyclization of (S)-reticuline to (S)-scoulerine. His174 was identified as a potentially important active site residue because its putative role for the stabilization of the reduced state of the flavin cofactor. It is also strictly conserved in the family of BBE-like oxidases. Here, we present a detailed biochemical and structural characterization of the BBE His174Ala variant supporting its role for catalysis as well as structural organization of the active site. Substantial changes in all kinetic parameters and a decrease in midpoint potential were observed for the BBE His174Ala variant protein. Moreover, the crystal structure of the BBE His174Ala showed significant structural rearrangements compared to wild type enzyme. Based on our findings, we propose that His174 is part of a hydrogen bonding network that stabilizes the negative charge at the N(1)-C(2)=O locus via interaction with the hydroxyl group at the C2' of the ribityl side chain. Hence replacement of this residue with alanine abolishes the stabilizing effect and results in drastically decreased kinetic parameters as well as a lower midpoint redox potential.

-	~~{{STRUCTURE_4ec3\| PDB=4ec3 \| SCENE= }}~~	+	Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme.,Wallner S, Winkler A, Riedl S, Dully C, Horvath S, Gruber K, Macheroux P Biochemistry. 2012 Jul 3. PMID:22757961<ref>PMID:22757961</ref>

-	~~===Structure of berberine bridge enzyme~~, ~~H174A variant in complex with (S)-reticuline===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_22757961}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[4ec3]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Eschscholzia_californica Eschscholzia californica]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022757961<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Eschscholzia californica]]		[[Category: Eschscholzia californica]]
	[[Category: Reticuline oxidase]]		[[Category: Reticuline oxidase]]

OCA at 06:35, 3 October 2012

OCA — Wed, 03 Oct 2012 06:35:24 GMT

←Older revision		Revision as of 06:35, 3 October 2012
Line 1:		Line 1:
-	[[Image:4ec3.~~jpg~~\|left\|200px]]	+	[[Image:4ec3.png\|left\|200px]]

	{{STRUCTURE_4ec3\| PDB=4ec3 \| SCENE= }}		{{STRUCTURE_4ec3\| PDB=4ec3 \| SCENE= }}

OCA at 05:24, 18 July 2012

OCA — Wed, 18 Jul 2012 05:24:38 GMT

←Older revision		Revision as of 05:24, 18 July 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4ec3.jpg\|left\|200px]]

-	~~The entry~~ 4ec3 ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4ec3\| PDB=4ec3 \| SCENE= }}

-	~~Authors: Winkler~~, ~~A., Macheroux, P., Gruber, K.~~	+	===Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline===

-	~~Description:~~ Structure ~~of berberine bridge enzyme, H174A variant in complex~~ with ~~(S)~~-~~reticuline~~	+	{{ABSTRACT_PUBMED_22757961}}
		+
		+	==About this Structure==
		+	[[4ec3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022757961</ref><references group="xtra"/>
		+	[[Category: Eschscholzia californica]]
		+	[[Category: Reticuline oxidase]]
		+	[[Category: Gruber, K.]]
		+	[[Category: Macheroux, P.]]
		+	[[Category: Winkler, A.]]
		+	[[Category: Bi-covalent flavinylation]]
		+	[[Category: Fad]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: P-cresol methyl hydroxylase superfamily]]

OCA at 06:40, 11 April 2012

OCA — Wed, 11 Apr 2012 06:40:39 GMT

←Older revision		Revision as of 06:40, 11 April 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ec3 is ON HOLD	+	The entry 4ec3 is ON HOLD until Paper Publication

	Authors: Winkler, A., Macheroux, P., Gruber, K.		Authors: Winkler, A., Macheroux, P., Gruber, K.

	Description: Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline		Description: Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline

OCA: Protected "4ec3" [edit=sysop:move=sysop]

OCA — Wed, 04 Apr 2012 05:48:02 GMT

Protected "4ec3" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:48, 4 April 2012

OCA: New page: '''Unreleased structure''' The entry 4ec3 is ON HOLD Authors: Winkler, A., Macheroux, P., Gruber, K. Description: Structure of berberine bridge enzyme, H174A variant in complex with (S...

OCA — Wed, 04 Apr 2012 05:48:01 GMT

New page: '''Unreleased structure''' The entry 4ec3 is ON HOLD Authors: Winkler, A., Macheroux, P., Gruber, K. Description: Structure of berberine bridge enzyme, H174A variant in complex with (S...

New page

'''Unreleased structure'''

The entry 4ec3 is ON HOLD

Authors: Winkler, A., Macheroux, P., Gruber, K.

Description: Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline