5awg - Revision history

OCA at 19:25, 29 May 2024

2024-05-29T19:25:13Z

←Older revision		Revision as of 19:25, 29 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5awg]] is a 8 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=5AWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWG FirstGlance]. <br>		<table><tr><td colspan='2'>[[5awg]] is a 8 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=5AWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 4.278Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [https://pdbe.org/5awg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [https://www.ebi.ac.uk/pdbsum/5awg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awg 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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [https://pdbe.org/5awg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [https://www.ebi.ac.uk/pdbsum/5awg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awg ProSAT]</span></td></tr>
	</table>		</table>

OCA at 06:27, 31 May 2023

2023-05-31T06:27:59Z

←Older revision		Revision as of 06:27, 31 May 2023
Line 3:		Line 3:
	<StructureSection load='5awg' size='340' side='right'caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>		<StructureSection load='5awg' size='340' side='right'caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5awg]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5awg]] is a 8 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=5AWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5awf\|5awf]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">sufB, ynhE, b1683, JW5273 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufD, ynhC, b1681, JW1671 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufC, ynhD, b1682, JW1672 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [https://pdbe.org/5awg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [https://www.ebi.ac.uk/pdbsum/5awg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awg 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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [https://pdbe.org/5awg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [https://www.ebi.ac.uk/pdbsum/5awg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SUFB_ECOLI SUFB_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12941942</ref> [[https://www.uniprot.org/uniprot/SUFC_ECOLI SUFC_ECOLI]] Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12554644</ref> <ref>PMID:12941942</ref> [[https://www.uniprot.org/uniprot/SUFD_ECOLI SUFD_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the FhuF protein.<ref>PMID:10322040</ref> <ref>PMID:12941942</ref>	+	[https://www.uniprot.org/uniprot/SUFB_ECOLI SUFB_ECOLI] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12941942</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hirabayashi, K]]	+	[[Category: Hirabayashi K]]
-	[[Category: Wada, K]]	+	[[Category: Wada K]]
-	~~[[Category: Abc atpase]]~~	+
-	~~[[Category: Abc protein]]~~	+
-	~~[[Category: Iron-sulfur cluster]]~~	+
-	~~[[Category: Iron-sulfur protein]]~~	+
-	~~[[Category: Transport protein-protein binding complex~~]]	+

OCA at 06:10, 11 August 2021

2021-08-11T06:10:05Z

←Older revision		Revision as of 06:10, 11 August 2021
Line 3:		Line 3:
	<StructureSection load='5awg' size='340' side='right'caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>		<StructureSection load='5awg' size='340' side='right'caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5awg]] is a 8 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=5AWG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5AWG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5awg]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5awf\|5awf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5awf\|5awf]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">sufB, ynhE, b1683, JW5273 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufD, ynhC, b1681, JW1671 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufC, ynhD, b1682, JW1672 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">sufB, ynhE, b1683, JW5273 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufD, ynhC, b1681, JW1671 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufC, ynhD, b1682, JW1672 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [~~http~~://pdbe.org/5awg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5awg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5awg 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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [https://pdbe.org/5awg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [https://www.ebi.ac.uk/pdbsum/5awg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SUFB_ECOLI SUFB_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12941942</ref> [[~~http~~://www.uniprot.org/uniprot/SUFC_ECOLI SUFC_ECOLI]] Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12554644</ref> <ref>PMID:12941942</ref> [[~~http~~://www.uniprot.org/uniprot/SUFD_ECOLI SUFD_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the FhuF protein.<ref>PMID:10322040</ref> <ref>PMID:12941942</ref>	+	[[https://www.uniprot.org/uniprot/SUFB_ECOLI SUFB_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12941942</ref> [[https://www.uniprot.org/uniprot/SUFC_ECOLI SUFC_ECOLI]] Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12554644</ref> <ref>PMID:12941942</ref> [[https://www.uniprot.org/uniprot/SUFD_ECOLI SUFD_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the FhuF protein.<ref>PMID:10322040</ref> <ref>PMID:12941942</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 09:53, 26 February 2020

2020-02-26T09:53:37Z

←Older revision		Revision as of 09:53, 26 February 2020
Line 1:		Line 1:

	==Crystal structure of Hg-bound SufB-SufC-SufD complex from Escherichia coli==		==Crystal structure of Hg-bound SufB-SufC-SufD complex from Escherichia coli==
-	<StructureSection load='5awg' size='340' side='right' caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>	+	<StructureSection load='5awg' size='340' side='right'caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5awg]] is a 8 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=5AWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AWG FirstGlance]. <br>		<table><tr><td colspan='2'>[[5awg]] is a 8 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=5AWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AWG FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Ecoli]]		[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Hirabayashi, K]]		[[Category: Hirabayashi, K]]
	[[Category: Wada, K]]		[[Category: Wada, K]]

OCA at 13:58, 16 November 2017

2017-11-16T13:58:36Z

←Older revision		Revision as of 13:58, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='5awg' size='340' side='right' caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>		<StructureSection load='5awg' size='340' side='right' caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5awg]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AWG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5awg]] is a 8 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=5AWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AWG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5awf\|5awf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5awf\|5awf]]</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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [http://pdbe.org/5awg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [http://www.ebi.ac.uk/pdbsum/5awg PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">sufB, ynhE, b1683, JW5273 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufD, ynhC, b1681, JW1671 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufC, ynhD, b1682, JW1672 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [http://pdbe.org/5awg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [http://www.ebi.ac.uk/pdbsum/5awg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5awg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Ecoli]]
	[[Category: Hirabayashi, K]]		[[Category: Hirabayashi, K]]
	[[Category: Wada, K]]		[[Category: Wada, K]]

OCA at 19:11, 20 February 2016

2016-02-20T19:11:25Z

←Older revision		Revision as of 19:11, 20 February 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5awg is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of Hg-bound SufB-SufC-SufD complex from Escherichia coli==
		+	<StructureSection load='5awg' size='340' side='right' caption='[[5awg]], [[Resolution\|resolution]] 4.28Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5awg]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AWG FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5awf\|5awf]]</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=5awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awg OCA], [http://pdbe.org/5awg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5awg RCSB], [http://www.ebi.ac.uk/pdbsum/5awg PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SUFB_ECOLI SUFB_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12941942</ref> [[http://www.uniprot.org/uniprot/SUFC_ECOLI SUFC_ECOLI]] Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12554644</ref> <ref>PMID:12941942</ref> [[http://www.uniprot.org/uniprot/SUFD_ECOLI SUFD_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the FhuF protein.<ref>PMID:10322040</ref> <ref>PMID:12941942</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	ATP-binding cassette (ABC)-type ATPases are chemomechanical engines involved in diverse biological pathways. Recent genomic information reveals that ABC ATPase domains/subunits act not only in ABC transporters and structural maintenance of chromosome proteins, but also in iron-sulfur (Fe-S) cluster biogenesis. A novel type of ABC protein, the SufBCD complex, functions in the biosynthesis of nascent Fe-S clusters in almost all Eubacteria and Archaea, as well as eukaryotic chloroplasts. In this study, we determined the first crystal structure of the Escherichia coli SufBCD complex, which exhibits the common architecture of ABC proteins: two ABC ATPase components (SufC) with function-specific components (SufB-SufD protomers). Biochemical and physiological analyses based on this structure provided critical insights into Fe-S cluster assembly and revealed a dynamic conformational change driven by ABC ATPase activity. We propose a molecular mechanism for the biogenesis of the Fe-S cluster in the SufBCD complex.

-	~~Authors:~~ Hirabayashi, K., ~~Wada~~, K.	+	Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis.,Hirabayashi K, Yuda E, Tanaka N, Katayama S, Iwasaki K, Matsumoto T, Kurisu G, Outten FW, Fukuyama K, Takahashi Y, Wada K J Biol Chem. 2015 Dec 11;290(50):29717-31. doi: 10.1074/jbc.M115.680934. Epub, 2015 Oct 15. PMID:26472926<ref>PMID:26472926</ref>

-	~~Description: Crystal structure~~ of Hg-~~bound SufB~~-~~SufC-SufD complex from Escherichia coli~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
		+	<div class="pdbe-citations 5awg" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Hirabayashi, K]]		[[Category: Hirabayashi, K]]
	[[Category: Wada, K]]		[[Category: Wada, K]]
		+	[[Category: Abc atpase]]
		+	[[Category: Abc protein]]
		+	[[Category: Iron-sulfur cluster]]
		+	[[Category: Iron-sulfur protein]]
		+	[[Category: Transport protein-protein binding complex]]

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←Older revision

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OCA: New page: '''Unreleased structure''' The entry 5awg is ON HOLD Authors: Hirabayashi, K., Wada, K. Description: Crystal structure of Hg-bound SufB-SufC-SufD complex from Escherichia coli [[Catego...

2015-07-15T11:43:11Z

New page: '''Unreleased structure''' The entry 5awg is ON HOLD Authors: Hirabayashi, K., Wada, K. Description: Crystal structure of Hg-bound SufB-SufC-SufD complex from Escherichia coli [[Catego...

New page

'''Unreleased structure'''

The entry 5awg is ON HOLD

Authors: Hirabayashi, K., Wada, K.

Description: Crystal structure of Hg-bound SufB-SufC-SufD complex from Escherichia coli
[[Category: Unreleased Structures]]
[[Category: Hirabayashi, K]]
[[Category: Wada, K]]