4edi - Revision history

OCA at 14:58, 14 March 2024

2024-03-14T14:58:25Z

←Older revision		Revision as of 14:58, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4edi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDI FirstGlance]. <br>		<table><tr><td colspan='2'>[[4edi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.998Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=4edi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edi OCA], [https://pdbe.org/4edi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edi RCSB], [https://www.ebi.ac.uk/pdbsum/4edi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edi 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=4edi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edi OCA], [https://pdbe.org/4edi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edi RCSB], [https://www.ebi.ac.uk/pdbsum/4edi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/EUTL_CLOPE EUTL_CLOPE]] A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. May be involved in cofactor diffusion across the BMC (Probable). Cobalamin is covalently bound to 1 subunit of the trimer on the concave (lumenal) face in a closed pore conformation; whether this is physiologically relevant is unclear (PubMed:25484204). The closed form has 3 very narrow channels (1.3 Angstrom at their narrowest) per trimer lined by acidic and aromatic residues; 2 ethanolamine molecules can bind in each channel, on either side of the constriction. Does not bind acetate, ethanol or acetyl phosphate, all of which are small molecules involved in ethanolamine metabolism (PubMed:25752492). Ethanolamine-binding has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (Probable).<ref>PMID:25484204</ref> <ref>PMID:25752492</ref> <ref>PMID:25484204</ref> <ref>PMID:25752492</ref> <ref>PMID:29717712</ref>	+	[https://www.uniprot.org/uniprot/EUTL_CLOPE EUTL_CLOPE] A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. May be involved in cofactor diffusion across the BMC (Probable). Cobalamin is covalently bound to 1 subunit of the trimer on the concave (lumenal) face in a closed pore conformation; whether this is physiologically relevant is unclear (PubMed:25484204). The closed form has 3 very narrow channels (1.3 Angstrom at their narrowest) per trimer lined by acidic and aromatic residues; 2 ethanolamine molecules can bind in each channel, on either side of the constriction. Does not bind acetate, ethanol or acetyl phosphate, all of which are small molecules involved in ethanolamine metabolism (PubMed:25752492). Ethanolamine-binding has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (Probable).<ref>PMID:25484204</ref> <ref>PMID:25752492</ref> <ref>PMID:25484204</ref> <ref>PMID:25752492</ref> <ref>PMID:29717712</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The ethanolamine utilization (Eut) microcompartment is a protein-based metabolic organelle that is strongly associated with pathogenesis in bacteria that inhabit the human gut. The exterior shell of this elaborate protein complex is composed from a few thousand copies of BMC-domain shell proteins, which form a semi-permeable diffusion barrier that provides the interior enzymes with substrates and cofactors while simultaneously retaining metabolic intermediates. The ability of this protein shell to regulate passage of substrate and cofactor molecules is critical for microcompartment function, but the details of how this diffusion barrier can allow the passage of large cofactors while still retaining small intermediates remain unclear. Previous work has revealed two conformations of the EutL shell protein, providing substantial evidence for a gated pore that might allow the passage of large cofactors. Here we report structural and biophysical evidence to show that ethanolamine, the substrate of the Eut microcompartment, acts as a negative allosteric regulator of EutL pore opening. Specifically, a series of X-ray crystal structures of EutL from Clostridium perfringens, along with equilibrium binding studies, reveal that ethanolamine binds to EutL at a site that exists in the closed-pore conformation and which is incompatible with opening of the large pore for cofactor transport. The allosteric mechanism we propose is consistent with the cofactor requirements of the Eut microcompartment, leading to a new model for EutL function. Furthermore, our results suggest the possibility of redox modulation of the allosteric mechanism, opening potentially new lines of investigation. This article is protected by copyright. All rights reserved.	+
-		+
-	An allosteric model for control of pore opening by substrate binding in the eutl microcompartment shell protein.,Thompson MC, Cascio D, Leibly DJ, Yeates TO Protein Sci. 2015 Mar 9. doi: 10.1002/pro.2672. PMID:25752492<ref>PMID:25752492</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4edi" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:06, 28 September 2022

2022-09-28T07:06:08Z

←Older revision		Revision as of 07:06, 28 September 2022
Line 1:		Line 1:
		+
	==Disulfide bonded EutL from Clostridium perfringens==		==Disulfide bonded EutL from Clostridium perfringens==
-	<StructureSection load='4edi' size='340' side='right' caption='[[4edi]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4edi' size='340' side='right'caption='[[4edi]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4edi]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus~~ perfringens~~" veillon and zuber 1898~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EDI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4edi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CPE0900, eutL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 "Bacillus perfringens" Veillon and Zuber 1898])</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=4edi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edi OCA], [https://pdbe.org/4edi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edi RCSB], [https://www.ebi.ac.uk/pdbsum/4edi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edi ProSAT]</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=4edi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edi OCA], [~~http~~://pdbe.org/4edi PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4edi RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4edi PDBsum]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/EUTL_CLOPE EUTL_CLOPE]] A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. May be involved in cofactor diffusion across the BMC (Probable). Cobalamin is covalently bound to 1 subunit of the trimer on the concave (lumenal) face in a closed pore conformation; whether this is physiologically relevant is unclear (PubMed:25484204). The closed form has 3 very narrow channels (1.3 Angstrom at their narrowest) per trimer lined by acidic and aromatic residues; 2 ethanolamine molecules can bind in each channel, on either side of the constriction. Does not bind acetate, ethanol or acetyl phosphate, all of which are small molecules involved in ethanolamine metabolism (PubMed:25752492). Ethanolamine-binding has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (Probable).<ref>PMID:25484204</ref> <ref>PMID:25752492</ref> <ref>PMID:25484204</ref> <ref>PMID:25752492</ref> <ref>PMID:29717712</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ perfringens ~~veillon and zuber 1898~~]]	+	[[Category: Clostridium perfringens]]
-	[[Category: ~~Cascio, D~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Crowley, C S~~]]	+	[[Category: Cascio D]]
-	[[Category: ~~Kopstein, J S~~]]	+	[[Category: Crowley CS]]
-	[[Category: ~~Thompson, M C~~]]	+	[[Category: Kopstein JS]]
-	[[Category: ~~Yeates, T O~~]]	+	[[Category: Thompson MC]]
-	[[Category: ~~Bacterial microcompartment]]~~	+	[[Category: Yeates TO]]
-	~~[[Category: Bmc shell protein]]~~	+
-	~~[[Category: Eut]]~~	+
-	~~[[Category: Transport protein~~]]	+

OCA at 09:06, 10 February 2016

2016-02-10T09:06:35Z

←Older revision		Revision as of 09:06, 10 February 2016
Line 2:		Line 2:
	<StructureSection load='4edi' size='340' side='right' caption='[[4edi]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4edi' size='340' side='right' caption='[[4edi]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4edi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Clostridium_perfringens Clostridium~~ perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EDI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4edi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EDI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CPE0900, eutL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 ~~Clostridium~~ perfringens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CPE0900, eutL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 "Bacillus perfringens" Veillon and Zuber 1898])</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=4edi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4edi RCSB], [http://www.ebi.ac.uk/pdbsum/4edi 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=4edi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edi OCA], [http://pdbe.org/4edi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4edi RCSB], [http://www.ebi.ac.uk/pdbsum/4edi PDBsum]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The ethanolamine utilization (Eut) microcompartment is a protein-based metabolic organelle that is strongly associated with pathogenesis in bacteria that inhabit the human gut. The exterior shell of this elaborate protein complex is composed from a few thousand copies of BMC-domain shell proteins, which form a semi-permeable diffusion barrier that provides the interior enzymes with substrates and cofactors while simultaneously retaining metabolic intermediates. The ability of this protein shell to regulate passage of substrate and cofactor molecules is critical for microcompartment function, but the details of how this diffusion barrier can allow the passage of large cofactors while still retaining small intermediates remain unclear. Previous work has revealed two conformations of the EutL shell protein, providing substantial evidence for a gated pore that might allow the passage of large cofactors. Here we report structural and biophysical evidence to show that ethanolamine, the substrate of the Eut microcompartment, acts as a negative allosteric regulator of EutL pore opening. Specifically, a series of X-ray crystal structures of EutL from Clostridium perfringens, along with equilibrium binding studies, reveal that ethanolamine binds to EutL at a site that exists in the closed-pore conformation and which is incompatible with opening of the large pore for cofactor transport. The allosteric mechanism we propose is consistent with the cofactor requirements of the Eut microcompartment, leading to a new model for EutL function. Furthermore, our results suggest the possibility of redox modulation of the allosteric mechanism, opening potentially new lines of investigation. This article is protected by copyright. All rights reserved.
		+
		+	An allosteric model for control of pore opening by substrate binding in the eutl microcompartment shell protein.,Thompson MC, Cascio D, Leibly DJ, Yeates TO Protein Sci. 2015 Mar 9. doi: 10.1002/pro.2672. PMID:25752492<ref>PMID:25752492</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4edi" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Clostridium~~ perfringens]]	+	[[Category: Bacillus perfringens veillon and zuber 1898]]
	[[Category: Cascio, D]]		[[Category: Cascio, D]]
	[[Category: Crowley, C S]]		[[Category: Crowley, C S]]

OCA at 08:18, 25 January 2015

2015-01-25T08:18:59Z

←Older revision		Revision as of 08:18, 25 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4edi\| PDB=4edi \| SCENE= }}~~	+	==Disulfide bonded EutL from Clostridium perfringens==
-	===Disulfide bonded EutL from Clostridium perfringens===	+	<StructureSection load='4edi' size='340' side='right' caption='[[4edi]], [[Resolution\|resolution]] 2.00Å' scene=''>
-		+	== Structural highlights ==
-	==~~About this Structure~~==	+	<table><tr><td colspan='2'>[[4edi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EDI FirstGlance]. <br>
-	[[4edi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA].	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CPE0900, eutL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 Clostridium perfringens])</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=4edi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4edi RCSB], [http://www.ebi.ac.uk/pdbsum/4edi PDBsum]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
	[[Category: Clostridium perfringens]]		[[Category: Clostridium perfringens]]
-	[[Category: Cascio, D.]]	+	[[Category: Cascio, D]]
-	[[Category: Crowley, C S.]]	+	[[Category: Crowley, C S]]
-	[[Category: Kopstein, J S.]]	+	[[Category: Kopstein, J S]]
-	[[Category: Thompson, M C.]]	+	[[Category: Thompson, M C]]
-	[[Category: Yeates, T O.]]	+	[[Category: Yeates, T O]]
	[[Category: Bacterial microcompartment]]		[[Category: Bacterial microcompartment]]
	[[Category: Bmc shell protein]]		[[Category: Bmc shell protein]]
	[[Category: Eut]]		[[Category: Eut]]
	[[Category: Transport protein]]		[[Category: Transport protein]]

OCA at 08:58, 27 March 2013

2013-03-27T08:58:42Z

←Older revision		Revision as of 08:58, 27 March 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4edi\| PDB=4edi \| SCENE= }}
		+	===Disulfide bonded EutL from Clostridium perfringens===

-	~~The entry~~ 4edi is ~~ON HOLD until Paper Publication~~	+	==About this Structure==
-		+	[[4edi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDI OCA].
-	~~Authors~~: ~~Thompson, M~~.C., Cascio, D., Crowley, C.S., Kopstein, J.S., Yeates, T.O.	+	[[Category: Clostridium perfringens]]
-		+	[[Category: Cascio, D.]]
-	~~Description~~: ~~Disulfide bonded EutL from Clostridium perfringens~~	+	[[Category: Crowley, C S.]]
		+	[[Category: Kopstein, J S.]]
		+	[[Category: Thompson, M C.]]
		+	[[Category: Yeates, T O.]]
		+	[[Category: Bacterial microcompartment]]
		+	[[Category: Bmc shell protein]]
		+	[[Category: Eut]]
		+	[[Category: Transport protein]]

OCA at 05:36, 23 May 2012

2012-05-23T05:36:27Z

←Older revision		Revision as of 05:36, 23 May 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Thompson, M.C., Cascio, D., Crowley, C.S., Kopstein, J.S., Yeates, T.O.		Authors: Thompson, M.C., Cascio, D., Crowley, C.S., Kopstein, J.S., Yeates, T.O.

	Description: Disulfide bonded EutL from Clostridium perfringens		Description: Disulfide bonded EutL from Clostridium perfringens

OCA at 06:40, 11 April 2012

2012-04-11T06:40:57Z

←Older revision		Revision as of 06:40, 11 April 2012
Line 3:		Line 3:
	The entry 4edi is ON HOLD		The entry 4edi is ON HOLD

-	Authors: Thompson, ~~Michael~~ C., Cascio, ~~Duilio~~, Crowley, ~~Christopher~~ S., Kopstein, ~~Jeffery~~ S., Yeates, ~~Todd~~ O.	+	Authors: Thompson, M.C., Cascio, D., Crowley, C.S., Kopstein, J.S., Yeates, T.O.

-	Description: Disulfide ~~Bonded~~ EutL from Clostridium ~~Perfringens~~	+	Description: Disulfide bonded EutL from Clostridium perfringens

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

2012-04-04T05:49:23Z

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

←Older revision

Revision as of 05:49, 4 April 2012

OCA: New page: '''Unreleased structure''' The entry 4edi is ON HOLD Authors: Thompson, Michael C., Cascio, Duilio, Crowley, Christopher S., Kopstein, Jeffery S., Yeates, Todd O. Description: Disulfid...

2012-04-04T05:49:22Z

New page: '''Unreleased structure''' The entry 4edi is ON HOLD Authors: Thompson, Michael C., Cascio, Duilio, Crowley, Christopher S., Kopstein, Jeffery S., Yeates, Todd O. Description: Disulfid...

New page

'''Unreleased structure'''

The entry 4edi is ON HOLD

Authors: Thompson, Michael C., Cascio, Duilio, Crowley, Christopher S., Kopstein, Jeffery S., Yeates, Todd O.

Description: Disulfide Bonded EutL from Clostridium Perfringens