4k39 - Revision history

OCA at 12:08, 1 March 2024

OCA — Fri, 01 Mar 2024 12:08:16 GMT

←Older revision		Revision as of 12:08, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4k39]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K39 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4k39]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K39 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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]] 1.783Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=4k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k39 OCA], [https://pdbe.org/4k39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k39 RCSB], [https://www.ebi.ac.uk/pdbsum/4k39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k39 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=4k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k39 OCA], [https://pdbe.org/4k39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k39 RCSB], [https://www.ebi.ac.uk/pdbsum/4k39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k39 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ANSME_CLOP1 ANSME_CLOP1] Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.<ref>PMID:16766528</ref> <ref>PMID:17335281</ref> <ref>PMID:18408004</ref>		[https://www.uniprot.org/uniprot/ANSME_CLOP1 ANSME_CLOP1] Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.<ref>PMID:16766528</ref> <ref>PMID:17335281</ref> <ref>PMID:18408004</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Arylsulfatases require a maturating enzyme to perform a co- or posttranslational modification to form a catalytically essential formylglycine (FGly) residue. In organisms that live aerobically, molecular oxygen is used enzymatically to oxidize cysteine to FGly. Under anaerobic conditions, S-adenosylmethionine (AdoMet) radical chemistry is used. Here we present the structures of an anaerobic sulfatase maturating enzyme (anSME), both with and without peptidyl-substrates, at 1.6-1.8 A resolution. We find that anSMEs differ from their aerobic counterparts in using backbone-based hydrogen-bonding patterns to interact with their peptidyl-substrates, leading to decreased sequence specificity. These anSME structures from Clostridium perfringens are also the first of an AdoMet radical enzyme that performs dehydrogenase chemistry. Together with accompanying mutagenesis data, a mechanistic proposal is put forth for how AdoMet radical chemistry is coopted to perform a dehydrogenation reaction. In the oxidation of cysteine or serine to FGly by anSME, we identify D277 and an auxiliary [4Fe-4S] cluster as the likely acceptor of the final proton and electron, respectively. D277 and both auxiliary clusters are housed in a cysteine-rich C-terminal domain, termed SPASM domain, that contains homology to approximately 1,400 other unique AdoMet radical enzymes proposed to use [4Fe-4S] clusters to ligate peptidyl-substrates for subsequent modification. In contrast to this proposal, we find that neither auxiliary cluster in anSME bind substrate, and both are fully ligated by cysteine residues. Instead, our structural data suggest that the placement of these auxiliary clusters creates a conduit for electrons to travel from the buried substrate to the protein surface.
-
-	X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification.,Goldman PJ, Grove TL, Sites LA, McLaughlin MI, Booker SJ, Drennan CL Proc Natl Acad Sci U S A. 2013 May 21;110(21):8519-24. doi:, 10.1073/pnas.1302417110. Epub 2013 May 6. PMID:23650368<ref>PMID:23650368</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4k39" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:38, 30 November 2022

OCA — Wed, 30 Nov 2022 11:38:16 GMT

←Older revision		Revision as of 11:38, 30 November 2022
Line 1:		Line 1:

	==Native anSMEcpe with bound AdoMet and Cp18Cys peptide==		==Native anSMEcpe with bound AdoMet and Cp18Cys peptide==
-	<StructureSection load='4k39' size='340' side='right' caption='[[4k39]], [[Resolution\|resolution]] 1.78Å' scene=''>	+	<StructureSection load='4k39' size='340' side='right'caption='[[4k39]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k39]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Clop1 Clop1~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K39 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4K39 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k39]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K39 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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">[[4k36\|4k36]], [[4k37\|4k37]], [[4k38\|4k38]]</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=4k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k39 OCA], [https://pdbe.org/4k39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k39 RCSB], [https://www.ebi.ac.uk/pdbsum/4k39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k39 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CPF_0616 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195103 CLOP1])~~</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=4k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k39 OCA], [~~http~~://pdbe.org/4k39 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4k39 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4k39 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4k39 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ANSME_CLOP1 ANSME_CLOP1]] Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.<ref>PMID:16766528</ref> <ref>PMID:17335281</ref> <ref>PMID:18408004</ref>	+	[https://www.uniprot.org/uniprot/ANSME_CLOP1 ANSME_CLOP1] Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.<ref>PMID:16766528</ref> <ref>PMID:17335281</ref> <ref>PMID:18408004</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: ~~Clop1~~]]	+	[[Category: Clostridium perfringens ATCC 13124]]
-	[[Category: ~~Drennan, C L~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Goldman, P J~~]]	+	[[Category: Drennan CL]]
-	[[Category: ~~Adomet radical fold]]~~	+	[[Category: Goldman PJ]]
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 22:16, 5 August 2016

OCA — Fri, 05 Aug 2016 22:16:39 GMT

←Older revision		Revision as of 22:16, 5 August 2016
Line 1:		Line 1:
		+
	==Native anSMEcpe with bound AdoMet and Cp18Cys peptide==		==Native anSMEcpe with bound AdoMet and Cp18Cys peptide==
	<StructureSection load='4k39' size='340' side='right' caption='[[4k39]], [[Resolution\|resolution]] 1.78Å' scene=''>		<StructureSection load='4k39' size='340' side='right' caption='[[4k39]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k39]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Clostridium_perfringens_atcc_13124 Clostridium perfringens atcc 13124~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K39 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k39]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clop1 Clop1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K39 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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">[[4k36\|4k36]], [[4k37\|4k37]], [[4k38\|4k38]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4k36\|4k36]], [[4k37\|4k37]], [[4k38\|4k38]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CPF_0616 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195103 ~~Clostridium perfringens ATCC 13124~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CPF_0616 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195103 CLOP1])</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=4k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k39 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k39 RCSB], [http://www.ebi.ac.uk/pdbsum/4k39 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=4k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k39 OCA], [http://pdbe.org/4k39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k39 RCSB], [http://www.ebi.ac.uk/pdbsum/4k39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k39 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4k39" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Clostridium perfringens atcc 13124~~]]	+	[[Category: Clop1]]
	[[Category: Drennan, C L]]		[[Category: Drennan, C L]]
	[[Category: Goldman, P J]]		[[Category: Goldman, P J]]
	[[Category: Adomet radical fold]]		[[Category: Adomet radical fold]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 06:19, 25 December 2014

OCA — Thu, 25 Dec 2014 06:19:07 GMT

←Older revision		Revision as of 06:19, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4k39\| PDB=4k39 \| SCENE= }}~~	+	==Native anSMEcpe with bound AdoMet and Cp18Cys peptide==
-	===Native anSMEcpe with bound AdoMet and Cp18Cys peptide===	+	<StructureSection load='4k39' size='340' side='right' caption='[[4k39]], [[Resolution\|resolution]] 1.78Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23650368}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4k39]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens_atcc_13124 Clostridium perfringens atcc 13124]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K39 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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">[[4k36\|4k36]], [[4k37\|4k37]], [[4k38\|4k38]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CPF_0616 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195103 Clostridium perfringens ATCC 13124])</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=4k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k39 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k39 RCSB], [http://www.ebi.ac.uk/pdbsum/4k39 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/ANSME_CLOP1 ANSME_CLOP1]] Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.<ref>PMID:16766528</ref> <ref>PMID:17335281</ref> <ref>PMID:18408004</ref>		[[http://www.uniprot.org/uniprot/ANSME_CLOP1 ANSME_CLOP1]] Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.<ref>PMID:16766528</ref> <ref>PMID:17335281</ref> <ref>PMID:18408004</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Arylsulfatases require a maturating enzyme to perform a co- or posttranslational modification to form a catalytically essential formylglycine (FGly) residue. In organisms that live aerobically, molecular oxygen is used enzymatically to oxidize cysteine to FGly. Under anaerobic conditions, S-adenosylmethionine (AdoMet) radical chemistry is used. Here we present the structures of an anaerobic sulfatase maturating enzyme (anSME), both with and without peptidyl-substrates, at 1.6-1.8 A resolution. We find that anSMEs differ from their aerobic counterparts in using backbone-based hydrogen-bonding patterns to interact with their peptidyl-substrates, leading to decreased sequence specificity. These anSME structures from Clostridium perfringens are also the first of an AdoMet radical enzyme that performs dehydrogenase chemistry. Together with accompanying mutagenesis data, a mechanistic proposal is put forth for how AdoMet radical chemistry is coopted to perform a dehydrogenation reaction. In the oxidation of cysteine or serine to FGly by anSME, we identify D277 and an auxiliary [4Fe-4S] cluster as the likely acceptor of the final proton and electron, respectively. D277 and both auxiliary clusters are housed in a cysteine-rich C-terminal domain, termed SPASM domain, that contains homology to approximately 1,400 other unique AdoMet radical enzymes proposed to use [4Fe-4S] clusters to ligate peptidyl-substrates for subsequent modification. In contrast to this proposal, we find that neither auxiliary cluster in anSME bind substrate, and both are fully ligated by cysteine residues. Instead, our structural data suggest that the placement of these auxiliary clusters creates a conduit for electrons to travel from the buried substrate to the protein surface.

-	~~==About this Structure==~~	+	X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification.,Goldman PJ, Grove TL, Sites LA, McLaughlin MI, Booker SJ, Drennan CL Proc Natl Acad Sci U S A. 2013 May 21;110(21):8519-24. doi:, 10.1073/pnas.1302417110. Epub 2013 May 6. PMID:23650368<ref>PMID:23650368</ref>
-	~~[[4k39]] is a 4 chain~~ structure ~~with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Clostridium_perfringens_atcc_13124 Clostridium perfringens atcc 13124]~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=4K39 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:023650368</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Clostridium perfringens atcc 13124]]		[[Category: Clostridium perfringens atcc 13124]]
-	[[Category: Drennan, C L.]]	+	[[Category: Drennan, C L]]
-	[[Category: Goldman, P J.]]	+	[[Category: Goldman, P J]]
	[[Category: Adomet radical fold]]		[[Category: Adomet radical fold]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 15:10, 19 June 2013

OCA — Wed, 19 Jun 2013 15:10:09 GMT

←Older revision		Revision as of 15:10, 19 June 2013
Line 1:		Line 1:
	{{STRUCTURE_4k39\| PDB=4k39 \| SCENE= }}		{{STRUCTURE_4k39\| PDB=4k39 \| SCENE= }}
	===Native anSMEcpe with bound AdoMet and Cp18Cys peptide===		===Native anSMEcpe with bound AdoMet and Cp18Cys peptide===
		+	{{ABSTRACT_PUBMED_23650368}}

	==Function==		==Function==
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	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023650368</ref><references group="xtra"/><references/>
	[[Category: Clostridium perfringens atcc 13124]]		[[Category: Clostridium perfringens atcc 13124]]
	[[Category: Drennan, C L.]]		[[Category: Drennan, C L.]]

OCA at 07:58, 8 May 2013

OCA — Wed, 08 May 2013 07:58:25 GMT

←Older revision		Revision as of 07:58, 8 May 2013
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-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4k39\| PDB=4k39 \| SCENE= }}
		+	===Native anSMEcpe with bound AdoMet and Cp18Cys peptide===

-	~~The entry 4k39~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/ANSME_CLOP1 ANSME_CLOP1]] Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.<ref>PMID:16766528</ref> <ref>PMID:17335281</ref> <ref>PMID:18408004</ref>

-	~~Authors~~: ~~Goldman, P~~.J.~~, Drennan, C~~.L.	+	==About this Structure==
		+	[[4k39]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens_atcc_13124 Clostridium perfringens atcc 13124]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K39 OCA].

-	~~Description~~: ~~Native anSMEcpe with bound AdoMet and Cp18Cys peptide~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Clostridium perfringens atcc 13124]]
		+	[[Category: Drennan, C L.]]
		+	[[Category: Goldman, P J.]]
		+	[[Category: Adomet radical fold]]
		+	[[Category: Oxidoreductase]]

OCA at 07:11, 2 May 2013

OCA — Thu, 02 May 2013 07:11:07 GMT

←Older revision		Revision as of 07:11, 2 May 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4k39 is ON HOLD	+	The entry 4k39 is ON HOLD until Paper Publication

	Authors: Goldman, P.J., Drennan, C.L.		Authors: Goldman, P.J., Drennan, C.L.

	Description: Native anSMEcpe with bound AdoMet and Cp18Cys peptide		Description: Native anSMEcpe with bound AdoMet and Cp18Cys peptide

OCA: Protected "4k39" [edit=sysop:move=sysop]

OCA — Wed, 17 Apr 2013 20:07:37 GMT

Protected "4k39" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:07, 17 April 2013

OCA: New page: '''Unreleased structure''' The entry 4k39 is ON HOLD Authors: Goldman, P.J., Drennan, C.L. Description: Native anSMEcpe with bound AdoMet and Cp18Cys peptide

OCA — Wed, 17 Apr 2013 20:07:36 GMT

New page: '''Unreleased structure''' The entry 4k39 is ON HOLD Authors: Goldman, P.J., Drennan, C.L. Description: Native anSMEcpe with bound AdoMet and Cp18Cys peptide

New page

'''Unreleased structure'''

The entry 4k39 is ON HOLD

Authors: Goldman, P.J., Drennan, C.L.

Description: Native anSMEcpe with bound AdoMet and Cp18Cys peptide