1qog - Revision history

OCA at 08:15, 14 February 2024

OCA — Wed, 14 Feb 2024 08:15:42 GMT

←Older revision		Revision as of 08:15, 14 February 2024
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	<StructureSection load='1qog' size='340' side='right'caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1qog' size='340' side='right'caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Anabaena_7120 Anabaena~~ 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [https://pdbe.org/1qog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [https://www.ebi.ac.uk/pdbsum/1qog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qog 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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [https://pdbe.org/1qog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [https://www.ebi.ac.uk/pdbsum/1qog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qog ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.	+	[https://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 20:
	</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=1qog 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=1qog ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	A combination of structural, thermodynamic, and transient kinetic data on wild-type and mutant Anabaena vegetative cell ferredoxins has been used to investigate the nature of the protein-protein interactions leading to electron transfer from reduced ferredoxin to oxidized ferredoxin:NADP+ reductase (FNR). We have determined the reduction potentials of wild-type vegetative ferredoxin, heterocyst ferredoxin, and 12 site-specific mutants at seven surface residues of vegetative ferredoxin, as well as the one- and two-electron reduction potentials of FNR, both alone and in complexes with wild-type and three mutant ferredoxins. X-ray crystallographic structure determinations have been carried out for six of the ferredoxin mutants. None of the mutants showed significant structural changes in the immediate vicinity of the [2Fe-2S] cluster, despite large decreases in electron-transfer reactivity (for E94K and S47A) and sizable increases in reduction potential (80 mV for E94K and 47 mV for S47A). Furthermore, the relatively small changes in Calpha backbone atom positions which were observed in these mutants do not correlate with the kinetic and thermodynamic properties. In sharp contrast to the S47A mutant, S47T retains electron-transfer activity, and its reduction potential is 100 mV more negative than that of the S47A mutant, implicating the importance of the hydrogen bond which exists between the side chain hydroxyl group of S47 and the side chain carboxyl oxygen of E94. Other ferredoxin mutations that alter both reduction potential and electron-transfer reactivity are E94Q, F65A, and F65I, whereas D62K, D68K, Q70K, E94D, and F65Y have reduction potentials and electron-transfer reactivity that are similar to those of wild-type ferredoxin. In electrostatic complexes with recombinant FNR, three of the kinetically impaired ferredoxin mutants, as did wild-type ferredoxin, induced large (approximately 40 mV) positive shifts in the reduction potential of the flavoprotein, thereby making electron transfer thermodynamically feasible. On the basis of these observations, we conclude that nonconservative mutations of three critical residues (S47, F65, and E94) on the surface of ferredoxin have large parallel effects on both the reduction potential and the electron-transfer reactivity of the [2Fe-2S] cluster and that the reduction potential changes are not the principal factor governing electron-transfer reactivity. Rather, the kinetic properties are most likely controlled by the specific orientations of the proteins within the transient electron-transfer complex.
-
-	Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants.,Hurley JK, Weber-Main AM, Stankovich MT, Benning MM, Thoden JB, Vanhooke JL, Holden HM, Chae YK, Xia B, Cheng H, Markley JL, Martinez-Julvez M, Gomez-Moreno C, Schmeits JL, Tollin G Biochemistry. 1997 Sep 16;36(37):11100-17. PMID:9287153<ref>PMID:9287153</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1qog" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Ferredoxin 3D structures\|Ferredoxin 3D structures]]		*[[Ferredoxin 3D structures\|Ferredoxin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Anabaena 7120]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Benning, M M~~]]	+	[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
-	[[Category: ~~Holden, H M~~]]	+	[[Category: Benning MM]]
-	[[Category: ~~Electron transport]]~~	+	[[Category: Holden HM]]
-	~~[[Category: Ferredoxin]]~~	+
-	~~[[Category: Iron-sulfur~~]]	+

OCA at 10:00, 15 September 2021

OCA — Wed, 15 Sep 2021 10:00:21 GMT

←Older revision		Revision as of 10:00, 15 September 2021
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	<StructureSection load='1qog' size='340' side='right'caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1qog' size='340' side='right'caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1QOG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [~~http~~://pdbe.org/1qog PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1qog PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1qog 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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [https://pdbe.org/1qog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [https://www.ebi.ac.uk/pdbsum/1qog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qog ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.	+	[[https://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:45, 4 December 2019

OCA — Wed, 04 Dec 2019 11:45:21 GMT

←Older revision		Revision as of 11:45, 4 December 2019
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	==FERREDOXIN MUTATION S47A==		==FERREDOXIN MUTATION S47A==
-	<StructureSection load='1qog' size='340' side='right' caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='1qog' size='340' side='right'caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[Ferredoxin\|Ferredoxin]]	+	*[[Ferredoxin 3D structures\|Ferredoxin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Anabaena 7120]]		[[Category: Anabaena 7120]]
		+	[[Category: Large Structures]]
	[[Category: Benning, M M]]		[[Category: Benning, M M]]
	[[Category: Holden, H M]]		[[Category: Holden, H M]]

OCA at 08:09, 28 February 2018

OCA — Wed, 28 Feb 2018 08:09:30 GMT

←Older revision		Revision as of 08:09, 28 February 2018
Line 1:		Line 1:
		+
	==FERREDOXIN MUTATION S47A==		==FERREDOXIN MUTATION S47A==
	<StructureSection load='1qog' size='340' side='right' caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1qog' size='340' side='right' caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [http://pdbe.org/1qog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [http://www.ebi.ac.uk/pdbsum/1qog 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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [http://pdbe.org/1qog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [http://www.ebi.ac.uk/pdbsum/1qog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qog ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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/qo/1qog_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/1qog_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 10:15, 9 February 2016

OCA — Tue, 09 Feb 2016 10:15:15 GMT

←Older revision		Revision as of 10:15, 9 February 2016
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=1qog ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:15, 10 September 2015

OCA — Thu, 10 Sep 2015 21:15:39 GMT

←Older revision		Revision as of 21:15, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1qog' size='340' side='right' caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1qog' size='340' side='right' caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Nostoc_sp. Nostoc sp.~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [http://www.ebi.ac.uk/pdbsum/1qog 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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [http://pdbe.org/1qog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [http://www.ebi.ac.uk/pdbsum/1qog PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~FER1_ANASP FER1_ANASP~~]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.	+	[[http://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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 1qog" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Nostoc sp~~]]	+	[[Category: Anabaena 7120]]
	[[Category: Benning, M M]]		[[Category: Benning, M M]]
	[[Category: Holden, H M]]		[[Category: Holden, H M]]

OCA at 06:11, 25 December 2014

OCA — Thu, 25 Dec 2014 06:11:55 GMT

←Older revision		Revision as of 06:11, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [http://www.ebi.ac.uk/pdbsum/1qog 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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [http://www.ebi.ac.uk/pdbsum/1qog PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FER1_ANASP FER1_ANASP]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Nostoc sp.]]	+	[[Category: Nostoc sp]]
-	[[Category: Benning, M M.]]	+	[[Category: Benning, M M]]
-	[[Category: Holden, H M.]]	+	[[Category: Holden, H M]]
	[[Category: Electron transport]]		[[Category: Electron transport]]
	[[Category: Ferredoxin]]		[[Category: Ferredoxin]]
	[[Category: Iron-sulfur]]		[[Category: Iron-sulfur]]

OCA at 23:34, 28 September 2014

OCA — Sun, 28 Sep 2014 23:34:30 GMT

←Older revision		Revision as of 23:34, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1qog.~~png\|left~~\|200px]]	+	==FERREDOXIN MUTATION S47A==
		+	<StructureSection load='1qog' size='340' side='right' caption='[[1qog]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<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=1qog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qog RCSB], [http://www.ebi.ac.uk/pdbsum/1qog 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/qo/1qog_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 ==
		+	A combination of structural, thermodynamic, and transient kinetic data on wild-type and mutant Anabaena vegetative cell ferredoxins has been used to investigate the nature of the protein-protein interactions leading to electron transfer from reduced ferredoxin to oxidized ferredoxin:NADP+ reductase (FNR). We have determined the reduction potentials of wild-type vegetative ferredoxin, heterocyst ferredoxin, and 12 site-specific mutants at seven surface residues of vegetative ferredoxin, as well as the one- and two-electron reduction potentials of FNR, both alone and in complexes with wild-type and three mutant ferredoxins. X-ray crystallographic structure determinations have been carried out for six of the ferredoxin mutants. None of the mutants showed significant structural changes in the immediate vicinity of the [2Fe-2S] cluster, despite large decreases in electron-transfer reactivity (for E94K and S47A) and sizable increases in reduction potential (80 mV for E94K and 47 mV for S47A). Furthermore, the relatively small changes in Calpha backbone atom positions which were observed in these mutants do not correlate with the kinetic and thermodynamic properties. In sharp contrast to the S47A mutant, S47T retains electron-transfer activity, and its reduction potential is 100 mV more negative than that of the S47A mutant, implicating the importance of the hydrogen bond which exists between the side chain hydroxyl group of S47 and the side chain carboxyl oxygen of E94. Other ferredoxin mutations that alter both reduction potential and electron-transfer reactivity are E94Q, F65A, and F65I, whereas D62K, D68K, Q70K, E94D, and F65Y have reduction potentials and electron-transfer reactivity that are similar to those of wild-type ferredoxin. In electrostatic complexes with recombinant FNR, three of the kinetically impaired ferredoxin mutants, as did wild-type ferredoxin, induced large (approximately 40 mV) positive shifts in the reduction potential of the flavoprotein, thereby making electron transfer thermodynamically feasible. On the basis of these observations, we conclude that nonconservative mutations of three critical residues (S47, F65, and E94) on the surface of ferredoxin have large parallel effects on both the reduction potential and the electron-transfer reactivity of the [2Fe-2S] cluster and that the reduction potential changes are not the principal factor governing electron-transfer reactivity. Rather, the kinetic properties are most likely controlled by the specific orientations of the proteins within the transient electron-transfer complex.

-	~~{{STRUCTURE_1qog\| PDB=1qog \| SCENE= }}~~	+	Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants.,Hurley JK, Weber-Main AM, Stankovich MT, Benning MM, Thoden JB, Vanhooke JL, Holden HM, Chae YK, Xia B, Cheng H, Markley JL, Martinez-Julvez M, Gomez-Moreno C, Schmeits JL, Tollin G Biochemistry. 1997 Sep 16;36(37):11100-17. PMID:9287153<ref>PMID:9287153</ref>

-	~~===FERREDOXIN MUTATION S47A===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9287153}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1qog]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Nostoc_sp~~. ~~Nostoc sp.]. Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA].~~	+

	==See Also==		==See Also==
	*[[Ferredoxin\|Ferredoxin]]		*[[Ferredoxin\|Ferredoxin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009287153<~~/~~ref~~><~~ref group="xtra">PMID:015173586</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Nostoc sp.]]		[[Category: Nostoc sp.]]
	[[Category: Benning, M M.]]		[[Category: Benning, M M.]]

OCA at 13:32, 20 October 2012

OCA — Sat, 20 Oct 2012 13:32:34 GMT

←Older revision		Revision as of 13:32, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1qog]] is a 2 chain structure ~~of [[Ferredoxin]]~~ with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA].	+	[[1qog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOG OCA].

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

OCA: Protected "1qog" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 12:18:27 GMT

Protected "1qog" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:18, 26 July 2012