3aeq - Revision history

OCA at 14:22, 1 November 2023

OCA — Wed, 01 Nov 2023 14:22:33 GMT

←Older revision		Revision as of 14:22, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3aeq' size='340' side='right'caption='[[3aeq]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='3aeq' size='340' side='right'caption='[[3aeq]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aeq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AEQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aeq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AEQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PMR:PROTOCHLOROPHYLLIDE'>PMR</scene>~~, ~~<scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.9Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[3aek\|3aek]], [[3aer\|3aer]], [[3aes\|3aes]], [[3aet\|3aet]], [[3aeu\|3aeu]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PMR:PROTOCHLOROPHYLLIDE'>PMR</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]<~~/b></td><td class="sblockDat">bchN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907]), bchB, bchK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907])</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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [https://pdbe.org/3aeq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [https://www.ebi.ac.uk/pdbsum/3aeq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aeq 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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [https://pdbe.org/3aeq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [https://www.ebi.ac.uk/pdbsum/3aeq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aeq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BCHN_RHOCB BCHN_RHOCB]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00352]<ref>PMID:18358835</ref> [[https://www.uniprot.org/uniprot/BCHB_RHOCB BCHB_RHOCB]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00353]<ref>PMID:18358835</ref>	+	[https://www.uniprot.org/uniprot/BCHN_RHOCB BCHN_RHOCB] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00352]<ref>PMID:18358835</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: Rhodonostoc capsulatum molisch 1907]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fujita, Y]]	+	[[Category: Rhodobacter capsulatus]]
-	[[Category: Kurisu, G]]	+	[[Category: Fujita Y]]
-	[[Category: Muraki, N]]	+	[[Category: Kurisu G]]
-	[[Category: Nomata, J]]	+	[[Category: Muraki N]]
-	[[Category: Shiba, T]]	+	[[Category: Nomata J]]
-	~~[[Category: Bacteriochlorophyll biosynthesis]]~~	+	[[Category: Shiba T]]
-	~~[[Category: Chlorophyll biosynthesis]]~~	+
-	~~[[Category: Iron/sulfur cluster]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Photosynthesis~~]]	+

OCA at 16:25, 22 December 2021

OCA — Wed, 22 Dec 2021 16:25:44 GMT

←Older revision		Revision as of 16:25, 22 December 2021
Line 1:		Line 1:

	==Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark==		==Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark==
-	<StructureSection load='3aeq' size='340' side='right' caption='[[3aeq]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='3aeq' size='340' side='right'caption='[[3aeq]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aeq]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3AEQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aeq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AEQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMR:PROTOCHLOROPHYLLIDE'>PMR</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PMR:PROTOCHLOROPHYLLIDE'>PMR</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aek\|3aek]], [[3aer\|3aer]], [[3aes\|3aes]], [[3aet\|3aet]], [[3aeu\|3aeu]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3aek\|3aek]], [[3aer\|3aer]], [[3aes\|3aes]], [[3aet\|3aet]], [[3aeu\|3aeu]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bchN ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907]), bchB, bchK ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bchN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907]), bchB, bchK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907])</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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [~~http~~://pdbe.org/3aeq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3aeq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3aeq 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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [https://pdbe.org/3aeq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [https://www.ebi.ac.uk/pdbsum/3aeq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aeq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BCHN_RHOCB BCHN_RHOCB]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00352]<ref>PMID:18358835</ref> [[~~http~~://www.uniprot.org/uniprot/BCHB_RHOCB BCHB_RHOCB]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00353]<ref>PMID:18358835</ref>	+	[[https://www.uniprot.org/uniprot/BCHN_RHOCB BCHN_RHOCB]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00352]<ref>PMID:18358835</ref> [[https://www.uniprot.org/uniprot/BCHB_RHOCB BCHB_RHOCB]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00353]<ref>PMID:18358835</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Rhodonostoc capsulatum molisch 1907]]		[[Category: Rhodonostoc capsulatum molisch 1907]]
		+	[[Category: Large Structures]]
	[[Category: Fujita, Y]]		[[Category: Fujita, Y]]
	[[Category: Kurisu, G]]		[[Category: Kurisu, G]]

OCA at 07:54, 24 October 2018

OCA — Wed, 24 Oct 2018 07:54:03 GMT

←Older revision		Revision as of 07:54, 24 October 2018
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/3aeq_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/3aeq_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 05:57, 5 August 2016

OCA — Fri, 05 Aug 2016 05:57:20 GMT

←Older revision		Revision as of 05:57, 5 August 2016
Line 1:		Line 1:
		+
	==Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark==		==Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark==
	<StructureSection load='3aeq' size='340' side='right' caption='[[3aeq]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='3aeq' size='340' side='right' caption='[[3aeq]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aeq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rhodobacter_capsulatus Rhodobacter capsulatus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AEQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aeq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AEQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMR:PROTOCHLOROPHYLLIDE'>PMR</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMR:PROTOCHLOROPHYLLIDE'>PMR</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aek\|3aek]], [[3aer\|3aer]], [[3aes\|3aes]], [[3aet\|3aet]], [[3aeu\|3aeu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aek\|3aek]], [[3aer\|3aer]], [[3aes\|3aes]], [[3aet\|3aet]], [[3aeu\|3aeu]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bchN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 ~~Rhodobacter capsulatus~~]), bchB, bchK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 ~~Rhodobacter capsulatus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bchN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907]), bchB, bchK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907])</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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [http://www.ebi.ac.uk/pdbsum/3aeq 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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [http://pdbe.org/3aeq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [http://www.ebi.ac.uk/pdbsum/3aeq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aeq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~BCHN_RHOCA BCHN_RHOCA~~]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00352]<ref>PMID:18358835</ref> [[http://www.uniprot.org/uniprot/~~BCHB_RHOCA BCHB_RHOCA~~]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00353]<ref>PMID:18358835</ref>	+	[[http://www.uniprot.org/uniprot/BCHN_RHOCB BCHN_RHOCB]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00352]<ref>PMID:18358835</ref> [[http://www.uniprot.org/uniprot/BCHB_RHOCB BCHB_RHOCB]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00353]<ref>PMID:18358835</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		Line 19:
	<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=3aeq 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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	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 3aeq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rhodobacter capsulatus~~]]	+	[[Category: Rhodonostoc capsulatum molisch 1907]]
	[[Category: Fujita, Y]]		[[Category: Fujita, Y]]
	[[Category: Kurisu, G]]		[[Category: Kurisu, G]]

OCA at 23:36, 24 December 2014

OCA — Wed, 24 Dec 2014 23:36:20 GMT

←Older revision		Revision as of 23:36, 24 December 2014
Line 8:		Line 8:
	<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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [http://www.ebi.ac.uk/pdbsum/3aeq 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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [http://www.ebi.ac.uk/pdbsum/3aeq PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BCHN_RHOCA BCHN_RHOCA]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00352]<ref>PMID:18358835</ref> [[http://www.uniprot.org/uniprot/BCHB_RHOCA BCHB_RHOCA]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00353]<ref>PMID:18358835</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Rhodobacter capsulatus]]		[[Category: Rhodobacter capsulatus]]
-	[[Category: Fujita, Y.]]	+	[[Category: Fujita, Y]]
-	[[Category: Kurisu, G.]]	+	[[Category: Kurisu, G]]
-	[[Category: Muraki, N.]]	+	[[Category: Muraki, N]]
-	[[Category: Nomata, J.]]	+	[[Category: Nomata, J]]
-	[[Category: Shiba, T.]]	+	[[Category: Shiba, T]]
	[[Category: Bacteriochlorophyll biosynthesis]]		[[Category: Bacteriochlorophyll biosynthesis]]
	[[Category: Chlorophyll biosynthesis]]		[[Category: Chlorophyll biosynthesis]]

OCA at 11:50, 29 October 2014

OCA — Wed, 29 Oct 2014 11:50:31 GMT

←Older revision		Revision as of 11:50, 29 October 2014
Line 1:		Line 1:
-	[[~~Image:~~3aeq.~~png~~\|~~left~~\|200px]]	+	==Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark==
		+	<StructureSection load='3aeq' size='340' side='right' caption='[[3aeq]], [[Resolution\|resolution]] 2.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3aeq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AEQ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMR:PROTOCHLOROPHYLLIDE'>PMR</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aek\|3aek]], [[3aer\|3aer]], [[3aes\|3aes]], [[3aet\|3aet]], [[3aeu\|3aeu]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">bchN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 Rhodobacter capsulatus]), bchB, bchK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 Rhodobacter capsulatus])</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=3aeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aeq RCSB], [http://www.ebi.ac.uk/pdbsum/3aeq 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/ae/3aeq_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 ==
		+	Photosynthetic organisms adopt two different strategies for the reduction of the C17 = C18 double bond of protochlorophyllide (Pchlide) to form chlorophyllide a, the direct precursor of chlorophyll a (refs 1-4). The first involves the activity of the light-dependent Pchlide oxidoreductase, and the second involves the light-independent (dark-operative) Pchlide oxidoreductase (DPOR). DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer), which are structurally related to nitrogenase Fe protein and MoFe protein, respectively. Here we report the crystal structure of the NB-protein of DPOR from Rhodobacter capsulatus at a resolution of 2.3A. As expected, the overall structure is similar to that of nitrogenase MoFe protein: each catalytic BchN-BchB unit contains one Pchlide and one iron-sulphur cluster (NB-cluster) coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific Pchlide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit. We propose a unique trans-specific reduction mechanism in which the distorted C17-propionate of Pchlide and an aspartate from BchB serve as proton donors for C18 and C17 of Pchlide, respectively. Intriguingly, the spatial arrangement of the NB-cluster and Pchlide is almost identical to that of the P-cluster and FeMo-cofactor in nitrogenase MoFe-protein, illustrating that a common architecture exists to reduce chemically stable multibonds of porphyrin and dinitrogen.

-	~~{{STRUCTURE_3aeq\| PDB=3aeq \| SCENE= }}~~	+	X-ray crystal structure of the light-independent protochlorophyllide reductase.,Muraki N, Nomata J, Ebata K, Mizoguchi T, Shiba T, Tamiaki H, Kurisu G, Fujita Y Nature. 2010 May 6;465(7294):110-4. PMID:20400946<ref>PMID:20400946</ref>

-	~~===Structure~~ of the ~~light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20400946}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[3aeq]] is a 4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:020400946<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Rhodobacter capsulatus]]		[[Category: Rhodobacter capsulatus]]
	[[Category: Fujita, Y.]]		[[Category: Fujita, Y.]]

OCA at 19:32, 7 January 2013

OCA — Mon, 07 Jan 2013 19:32:55 GMT

←Older revision		Revision as of 19:32, 7 January 2013
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	[[Image:3aeq.png\|left\|200px]]		[[Image:3aeq.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3aeq", 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_3aeq\| PDB=3aeq \| SCENE= }}		{{STRUCTURE_3aeq\| PDB=3aeq \| SCENE= }}

	===Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark===		===Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20400946}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20400946 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_20400946}}		{{ABSTRACT_PUBMED_20400946}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20400946~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020400946</ref><references group="xtra"/>
	[[Category: Rhodobacter capsulatus]]		[[Category: Rhodobacter capsulatus]]
	[[Category: Fujita, Y.]]		[[Category: Fujita, Y.]]

OCA: Protected "3aeq" [edit=sysop:move=sysop]

OCA — Sun, 02 Jan 2011 03:14:42 GMT

Protected "3aeq" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:14, 2 January 2011

OCA at 03:14, 2 January 2011

OCA — Sun, 02 Jan 2011 03:14:41 GMT

←Older revision		Revision as of 03:14, 2 January 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3aeq.png\|left\|200px]]		[[Image:3aeq.png\|left\|200px]]

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	==About this Structure==		==About this Structure==
-	~~3AEQ~~ is a 4 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA].	+	[[3aeq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA].

	==Reference==		==Reference==
Line 35:		Line 34:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Photosynthesis]]		[[Category: Photosynthesis]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:00:05 2010''

OCA at 06:00, 20 May 2010

OCA — Thu, 20 May 2010 06:00:06 GMT

←Older revision		Revision as of 06:00, 20 May 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3aeq.~~jpg~~\|left\|200px]]	+	[[Image:3aeq.png\|left\|200px]]

	<!--		<!--
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	===Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark===		===Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20400946}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20400946 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20400946}}

	==About this Structure==		==About this Structure==
	3AEQ is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA].		3AEQ is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEQ OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20400946</ref><references group="xtra"/>
	[[Category: Rhodobacter capsulatus]]		[[Category: Rhodobacter capsulatus]]
	[[Category: Fujita, Y.]]		[[Category: Fujita, Y.]]
Line 27:		Line 36:
	[[Category: Photosynthesis]]		[[Category: Photosynthesis]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Apr 21 10~~:50:18 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:00:05 2010''