4g39 - Revision history

OCA at 11:25, 1 March 2024

2024-03-01T11:25:23Z

←Older revision		Revision as of 11:25, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G39 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G39 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</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]] 2.4Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [https://pdbe.org/4g39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [https://www.ebi.ac.uk/pdbsum/4g39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g39 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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [https://pdbe.org/4g39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [https://www.ebi.ac.uk/pdbsum/4g39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g39 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/CYSI_ECOLI CYSI_ECOLI] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.[HAMAP-Rule:MF_01540]		[https://www.uniprot.org/uniprot/CYSI_ECOLI CYSI_ECOLI] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.[HAMAP-Rule:MF_01540]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide. The active site, found in the hemoprotein subunit (SiRHP), sits on the distal face of a negatively charged porphyrinoid called siroheme whose central iron atom is coupled to a proximal Fe(4)S(4) cluster. Four positively charged amino acids are positioned around the active site cavity. Together, these two arginines (R83 and R153) and two lysines (K215 and K217) mitigate the negative charge on the siroheme macrocycle. They also serve as a cage around the distally bound anion that tightens when substrate binds and an active site loop clamps down. Structures of native SiRHP point to these amino acids as being important, but their specific roles are ill-defined. Here, we have altered those four active site amino acids and one amino acid on the flexible loop (N149) to probe their roles in SiRHP activity. None of these positively charged residues is required for electron transfer, but only R83S and N149W variants can produce a fully reduced product. By measuring the electrons used per unit of reduced sulfur released, we show that K215, R153, and K217 are responsible for intermediate and late proton transfers, whereas N149 and R153 play a role in the structure of the flexible loop that controls anion binding and release. R83 is primarily responsible for siroheme binding. Together, the activities and structures of these variants reveal specific roles for each in anion binding and in coupled proton transfer that facilitates electron transfer.
-
-	Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism for Coordinated Electron and Proton Transfer.,Smith KW, Stroupe ME Biochemistry. 2012 Nov 29. PMID:23153334<ref>PMID:23153334</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4g39" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 20:22, 19 October 2022

2022-10-19T20:22:42Z

←Older revision		Revision as of 20:22, 19 October 2022
Line 3:		Line 3:
	<StructureSection load='4g39' size='340' side='right'caption='[[4g39]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4g39' size='340' side='right'caption='[[4g39]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4G39 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G39 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aop\|1aop]], [[4g38\|4g38]]</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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [https://pdbe.org/4g39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [https://www.ebi.ac.uk/pdbsum/4g39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g39 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b2763, cysI, JW2733 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfite_reductase_(NADPH) Sulfite reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.2 1.8.1.2] </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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [~~http~~://pdbe.org/4g39 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4g39 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4g39 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CYSI_ECOLI CYSI_ECOLI]] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.[HAMAP-Rule:MF_01540]	+	[https://www.uniprot.org/uniprot/CYSI_ECOLI CYSI_ECOLI] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.[HAMAP-Rule:MF_01540]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Smith~~, K W~~]]	+	[[Category: Smith KW]]
-	[[Category: Stroupe~~, M E]]~~	+	[[Category: Stroupe ME]]
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Snirr]]~~	+
-	~~[[Category: Sulfite reductase flavoprotein~~]]	+

OCA at 11:54, 17 July 2019

2019-07-17T11:54:03Z

←Older revision		Revision as of 11:54, 17 July 2019
Line 1:		Line 1:

	==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer==		==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer==
-	<StructureSection load='4g39' size='340' side='right' caption='[[4g39]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='4g39' size='340' side='right'caption='[[4g39]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G39 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G39 FirstGlance]. <br>
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Ecoli]]		[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Smith, K W]]		[[Category: Smith, K W]]
	[[Category: Stroupe, M E]]		[[Category: Stroupe, M E]]

OCA at 17:52, 5 August 2016

2016-08-05T17:52:08Z

←Older revision		Revision as of 17:52, 5 August 2016
Line 1:		Line 1:
		+
	==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer==		==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer==
	<StructureSection load='4g39' size='340' side='right' caption='[[4g39]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4g39' size='340' side='right' caption='[[4g39]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_k-12 Escherichia coli k-12~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G39 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G39 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aop\|1aop]], [[4g38\|4g38]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aop\|1aop]], [[4g38\|4g38]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b2763, cysI, JW2733 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b2763, cysI, JW2733 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfite_reductase_(NADPH) Sulfite reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.2 1.8.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfite_reductase_(NADPH) Sulfite reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.2 1.8.1.2] </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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [http://www.ebi.ac.uk/pdbsum/4g39 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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [http://pdbe.org/4g39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [http://www.ebi.ac.uk/pdbsum/4g39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g39 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 4g39" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli k-12~~]]	+	[[Category: Ecoli]]
	[[Category: Smith, K W]]		[[Category: Smith, K W]]
	[[Category: Stroupe, M E]]		[[Category: Stroupe, M E]]

OCA at 04:35, 25 December 2014

2014-12-25T04:35:48Z

←Older revision		Revision as of 04:35, 25 December 2014
Line 9:		Line 9:
	<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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [http://www.ebi.ac.uk/pdbsum/4g39 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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [http://www.ebi.ac.uk/pdbsum/4g39 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CYSI_ECOLI CYSI_ECOLI]] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.[HAMAP-Rule:MF_01540]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:32, 9 December 2014

2014-12-09T17:32:46Z

←Older revision		Revision as of 17:32, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4g39.~~png~~\|~~left~~\|~~200px~~]]	+	==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer==
		+	<StructureSection load='4g39' size='340' side='right' caption='[[4g39]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G39 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aop\|1aop]], [[4g38\|4g38]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b2763, cysI, JW2733 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfite_reductase_(NADPH) Sulfite reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.2 1.8.1.2] </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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [http://www.ebi.ac.uk/pdbsum/4g39 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide. The active site, found in the hemoprotein subunit (SiRHP), sits on the distal face of a negatively charged porphyrinoid called siroheme whose central iron atom is coupled to a proximal Fe(4)S(4) cluster. Four positively charged amino acids are positioned around the active site cavity. Together, these two arginines (R83 and R153) and two lysines (K215 and K217) mitigate the negative charge on the siroheme macrocycle. They also serve as a cage around the distally bound anion that tightens when substrate binds and an active site loop clamps down. Structures of native SiRHP point to these amino acids as being important, but their specific roles are ill-defined. Here, we have altered those four active site amino acids and one amino acid on the flexible loop (N149) to probe their roles in SiRHP activity. None of these positively charged residues is required for electron transfer, but only R83S and N149W variants can produce a fully reduced product. By measuring the electrons used per unit of reduced sulfur released, we show that K215, R153, and K217 are responsible for intermediate and late proton transfers, whereas N149 and R153 play a role in the structure of the flexible loop that controls anion binding and release. R83 is primarily responsible for siroheme binding. Together, the activities and structures of these variants reveal specific roles for each in anion binding and in coupled proton transfer that facilitates electron transfer.

-	~~{{STRUCTURE_4g39\| PDB=4g39 \| SCENE= }}~~	+	Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism for Coordinated Electron and Proton Transfer.,Smith KW, Stroupe ME Biochemistry. 2012 Nov 29. PMID:23153334<ref>PMID:23153334</ref>

-	~~===Mutational analysis~~ of ~~sulfite reductase hemoprotein reveals~~ the ~~mechanism for coordinated electron and proton transfer===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_23153334}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[4g39]] is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA].~~	+	</StructureSection>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
-	[[Category: Smith, K W.]]	+	[[Category: Smith, K W]]
-	[[Category: Stroupe, M E.]]	+	[[Category: Stroupe, M E]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Snirr]]		[[Category: Snirr]]
	[[Category: Sulfite reductase flavoprotein]]		[[Category: Sulfite reductase flavoprotein]]

OCA at 12:55, 6 March 2013

2013-03-06T12:55:42Z

←Older revision		Revision as of 12:55, 6 March 2013
Line 1:		Line 1:
-	[[Image:4g39.~~jpg~~\|left\|200px]]	+	[[Image:4g39.png\|left\|200px]]

	{{STRUCTURE_4g39\| PDB=4g39 \| SCENE= }}		{{STRUCTURE_4g39\| PDB=4g39 \| SCENE= }}

OCA at 09:22, 2 January 2013

2013-01-02T09:22:17Z

←Older revision		Revision as of 09:22, 2 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4g39.jpg\|left\|200px]]

-	~~The entry~~ 4g39 ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4g39\| PDB=4g39 \| SCENE= }}

-	~~Authors: Smith, K.W., Stroupe, M.E.~~	+	===Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer===

-	~~Description~~: ~~Mutational analysis of sulfite~~ reductase ~~hemoprotein reveals the mechanism for coordinated electron and proton transfer~~	+	{{ABSTRACT_PUBMED_23153334}}
		+
		+	==About this Structure==
		+	[[4g39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA].
		+	[[Category: Escherichia coli k-12]]
		+	[[Category: Smith, K W.]]
		+	[[Category: Stroupe, M E.]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Snirr]]
		+	[[Category: Sulfite reductase flavoprotein]]

OCA at 05:22, 15 August 2012

2012-08-15T05:22:06Z

←Older revision		Revision as of 05:22, 15 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4g39 is ON HOLD	+	The entry 4g39 is ON HOLD until Paper Publication

	Authors: Smith, K.W., Stroupe, M.E.		Authors: Smith, K.W., Stroupe, M.E.

	Description: Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer		Description: Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer

OCA: Protected "4g39" [edit=sysop:move=sysop]

2012-07-25T06:50:51Z

Protected "4g39" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:50, 25 July 2012