8ajj - Revision history

OCA at 08:12, 7 February 2024

OCA — Wed, 07 Feb 2024 08:12:21 GMT

←Older revision		Revision as of 08:12, 7 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8ajj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AJJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[8ajj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AJJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</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=8ajj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ajj OCA], [https://pdbe.org/8ajj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ajj RCSB], [https://www.ebi.ac.uk/pdbsum/8ajj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ajj 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=8ajj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ajj OCA], [https://pdbe.org/8ajj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ajj RCSB], [https://www.ebi.ac.uk/pdbsum/8ajj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ajj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/A0A266CGC0_STAAU A0A266CGC0_STAAU]		[https://www.uniprot.org/uniprot/A0A266CGC0_STAAU A0A266CGC0_STAAU]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The major pathogen Staphylococcus aureus has to cope with host-derived oxidative stress to cause infections in humans. Here, we report that S. aureus tolerates high concentrations of hypothiocyanous acid (HOSCN), a key antimicrobial oxidant produced in the respiratory tract. We discovered that the flavoprotein disulfide reductase (FDR) MerA protects S. aureus from this oxidant by functioning as a HOSCN reductase, with its deletion sensitizing bacteria to HOSCN. Crystal structures of homodimeric MerA (2.4 A) with a Cys(43) -Cys(48) intramolecular disulfide, and reduced MerACys(43) S (1.6 A) showed the FAD cofactor close to the active site, supporting that MerA functions as a group I FDR. MerA is controlled by the redox-sensitive repressor HypR, which we show to be oxidized to intermolecular disulfides under HOSCN stress, resulting in its inactivation and derepression of merA transcription to promote HOSCN tolerance. Our study highlights the HOSCN tolerance of S. aureus and characterizes the structure and function of MerA as a major HOSCN defense mechanism. Crippling the capacity to respond to HOSCN may be a novel strategy for treating S. aureus infections.
-
-	MerA functions as a hypothiocyanous acid reductase and defense mechanism in Staphylococcus aureus.,Shearer HL, Loi VV, Weiland P, Bange G, Altegoer F, Hampton MB, Antelmann H, Dickerhof N Mol Microbiol. 2023 Feb 13. doi: 10.1111/mmi.15035. PMID:36779383<ref>PMID:36779383</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8ajj" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:00, 2 March 2023

OCA — Thu, 02 Mar 2023 06:00:48 GMT

←Older revision		Revision as of 06:00, 2 March 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8ajj is ~~ON HOLD until Paper~~ Publication	+	==Crystal structure of the disulfide reductase MerA from Staphylococcus aureus==
		+	<StructureSection load='8ajj' size='340' side='right'caption='[[8ajj]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8ajj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AJJ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</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=8ajj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ajj OCA], [https://pdbe.org/8ajj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ajj RCSB], [https://www.ebi.ac.uk/pdbsum/8ajj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ajj ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/A0A266CGC0_STAAU A0A266CGC0_STAAU]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The major pathogen Staphylococcus aureus has to cope with host-derived oxidative stress to cause infections in humans. Here, we report that S. aureus tolerates high concentrations of hypothiocyanous acid (HOSCN), a key antimicrobial oxidant produced in the respiratory tract. We discovered that the flavoprotein disulfide reductase (FDR) MerA protects S. aureus from this oxidant by functioning as a HOSCN reductase, with its deletion sensitizing bacteria to HOSCN. Crystal structures of homodimeric MerA (2.4 A) with a Cys(43) -Cys(48) intramolecular disulfide, and reduced MerACys(43) S (1.6 A) showed the FAD cofactor close to the active site, supporting that MerA functions as a group I FDR. MerA is controlled by the redox-sensitive repressor HypR, which we show to be oxidized to intermolecular disulfides under HOSCN stress, resulting in its inactivation and derepression of merA transcription to promote HOSCN tolerance. Our study highlights the HOSCN tolerance of S. aureus and characterizes the structure and function of MerA as a major HOSCN defense mechanism. Crippling the capacity to respond to HOSCN may be a novel strategy for treating S. aureus infections.

-	~~Authors: Weiland~~, P., ~~Altegoer~~, F., ~~Bange~~, G.	+	MerA functions as a hypothiocyanous acid reductase and defense mechanism in Staphylococcus aureus.,Shearer HL, Loi VV, Weiland P, Bange G, Altegoer F, Hampton MB, Antelmann H, Dickerhof N Mol Microbiol. 2023 Feb 13. doi: 10.1111/mmi.15035. PMID:36779383<ref>PMID:36779383</ref>

-	~~Description: Crystal structure~~ of the ~~disulfide reductase MerA from Staphylococcus aureus~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: ~~Bange, G~~]]	+	<div class="pdbe-citations 8ajj" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Weiland, P~~]]	+	== References ==
-	[[Category: ~~Altegoer, F~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Staphylococcus aureus]]
		+	[[Category: Altegoer F]]
		+	[[Category: Bange G]]
		+	[[Category: Weiland P]]

OCA at 05:22, 31 August 2022

OCA — Wed, 31 Aug 2022 05:22:49 GMT

←Older revision		Revision as of 05:22, 31 August 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8ajj is ON HOLD	+	The entry 8ajj is ON HOLD until Paper Publication

	Authors: Weiland, P., Altegoer, F., Bange, G.		Authors: Weiland, P., Altegoer, F., Bange, G.

OCA: Protected "8ajj" [edit=sysop:move=sysop]

OCA — Wed, 03 Aug 2022 03:50:34 GMT

Protected "8ajj" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:50, 3 August 2022

OCA: New page: '''Unreleased structure''' The entry 8ajj is ON HOLD Authors: Weiland, P., Altegoer, F., Bange, G. Description: Crystal structure of the disulfide reductase MerA from Staphylococcus au...

OCA — Wed, 03 Aug 2022 03:50:33 GMT

New page: '''Unreleased structure''' The entry 8ajj is ON HOLD Authors: Weiland, P., Altegoer, F., Bange, G. Description: Crystal structure of the disulfide reductase MerA from Staphylococcus au...

New page

'''Unreleased structure'''

The entry 8ajj is ON HOLD

Authors: Weiland, P., Altegoer, F., Bange, G.

Description: Crystal structure of the disulfide reductase MerA from Staphylococcus aureus
[[Category: Unreleased Structures]]
[[Category: Bange, G]]
[[Category: Weiland, P]]
[[Category: Altegoer, F]]