3lc9 - Revision history

OCA at 06:35, 19 July 2023

2023-07-19T06:35:40Z

←Older revision		Revision as of 06:35, 19 July 2023
Line 3:		Line 3:
	<StructureSection load='3lc9' size='340' side='right'caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='3lc9' size='340' side='right'caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Castor_bean Castor bean~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.28Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[3bjg\|3bjg]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22]~~ </~~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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [https://pdbe.org/3lc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [https://www.ebi.ac.uk/pdbsum/3lc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lc9 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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [https://pdbe.org/3lc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [https://www.ebi.ac.uk/pdbsum/3lc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lc9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/RICI_RICCO RICI_RICCO]] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).	+	[https://www.uniprot.org/uniprot/RICI_RICCO RICI_RICCO] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 21:

	==See Also==		==See Also==
-	*[[Ricin\|Ricin]]	+	*[[Ricin 3D structures\|Ricin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Castor bean]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~RRNA N-glycosylase~~]]	+	[[Category: Ricinus communis]]
-	[[Category: Compton~~, J R~~]]	+	[[Category: Compton JR]]
-	[[Category: Legler~~, P M~~]]	+	[[Category: Legler PM]]
-	[[Category: Millard~~, C B]]~~	+	[[Category: Millard CB]]
-	~~[[Category: Disulfide bond]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Immunogen]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Plant defense]]~~	+
-	~~[[Category: Protein synthesis inhibitor]]~~	+
-	~~[[Category: Ricin]]~~	+
-	~~[[Category: Toxin~~]]	+

OCA at 12:32, 13 October 2021

2021-10-13T12:32:54Z

←Older revision		Revision as of 12:32, 13 October 2021
Line 3:		Line 3:
	<StructureSection load='3lc9' size='340' side='right'caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='3lc9' size='340' side='right'caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bjg\|3bjg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bjg\|3bjg]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [~~http~~://pdbe.org/3lc9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3lc9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3lc9 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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [https://pdbe.org/3lc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [https://www.ebi.ac.uk/pdbsum/3lc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lc9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RICI_RICCO RICI_RICCO]] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).	+	[[https://www.uniprot.org/uniprot/RICI_RICCO RICI_RICCO]] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:05, 7 October 2020

2020-10-07T07:05:51Z

←Older revision		Revision as of 07:05, 7 October 2020
Line 1:		Line 1:

	==Ricin A-chain variant 1-33/44-198 with engineered disulfide bond==		==Ricin A-chain variant 1-33/44-198 with engineered disulfide bond==
-	<StructureSection load='3lc9' size='340' side='right' caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>	+	<StructureSection load='3lc9' size='340' side='right'caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bjg\|3bjg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bjg\|3bjg]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [http://pdbe.org/3lc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [http://www.ebi.ac.uk/pdbsum/3lc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lc9 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [http://pdbe.org/3lc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [http://www.ebi.ac.uk/pdbsum/3lc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lc9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Castor bean]]		[[Category: Castor bean]]
		+	[[Category: Large Structures]]
	[[Category: RRNA N-glycosylase]]		[[Category: RRNA N-glycosylase]]
	[[Category: Compton, J R]]		[[Category: Compton, J R]]

OCA at 17:49, 5 August 2016

2016-08-05T17:49:19Z

←Older revision		Revision as of 17:49, 5 August 2016
Line 1:		Line 1:
		+
	==Ricin A-chain variant 1-33/44-198 with engineered disulfide bond==		==Ricin A-chain variant 1-33/44-198 with engineered disulfide bond==
	<StructureSection load='3lc9' size='340' side='right' caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='3lc9' size='340' side='right' caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Ricinus_communis Ricinus communis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bjg\|3bjg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bjg\|3bjg]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [http://www.ebi.ac.uk/pdbsum/3lc9 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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [http://pdbe.org/3lc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [http://www.ebi.ac.uk/pdbsum/3lc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lc9 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 3lc9" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ricinus communis~~]]	+	[[Category: Castor bean]]
	[[Category: RRNA N-glycosylase]]		[[Category: RRNA N-glycosylase]]
	[[Category: Compton, J R]]		[[Category: Compton, J R]]

OCA at 04:34, 25 December 2014

2014-12-25T04:34:51Z

←Older revision		Revision as of 04:34, 25 December 2014
Line 8:		Line 8:
	<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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [http://www.ebi.ac.uk/pdbsum/3lc9 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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [http://www.ebi.ac.uk/pdbsum/3lc9 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RICI_RICCO RICI_RICCO]] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 09:42, 9 December 2014

2014-12-09T09:42:11Z

←Older revision		Revision as of 09:42, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3lc9.~~png~~\|~~left~~\|~~200px~~]]	+	==Ricin A-chain variant 1-33/44-198 with engineered disulfide bond==
		+	<StructureSection load='3lc9' size='340' side='right' caption='[[3lc9]], [[Resolution\|resolution]] 2.28Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3lc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LC9 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bjg\|3bjg]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </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=3lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lc9 RCSB], [http://www.ebi.ac.uk/pdbsum/3lc9 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	RTA1-33/44-198 is a catalytically inactive, single-domain derivative of the ricin toxin A-chain (RTA) engineered to serve as a stable protein scaffold for presentation of native immunogenic epitopes (Olson et al., Protein Eng Des Sel 2004;17:391-397). To improve the stability and solubility of RTA1-33/44-198 further, we have undertaken the design challenge of introducing a disulfide (SS) bond. Nine pairs of residues were selected for placement of the SS-bond based on molecular dynamics simulation studies of the modeled single-domain chain. Disulfide formation at either of two positions (R48C/T77C or V49C/E99C) involving a specific surface loop (44-55) increased the protein melting temperature by ~5 degrees C compared with RTA1-33/44-198 and by ~13 degrees C compared with RTA. Prolonged stability studies of the R48C/T77C variant (> 60 days at 37 degrees C, pH 7.4) confirmed a > 40% reduction in self-aggregation compared with RTA1-33/44-198 lacking the SS-bond. The R48C/T77C variant retained affinity for anti-RTA antibodies capable of neutralizing ricin toxin, including a monoclonal that recognizes a human B-cell epitope. Introduction of either R48C/T77C or V49C/E99C promoted crystallization of RTA1-33/44-198, and the X-ray structures of the variants were solved to 2.3 A or 2.1 A resolution, respectively. The structures confirm formation of an intramolecular SS-bond, and reveal a single-domain fold that is significantly reduced in volume compared with RTA. Loop 44 to 55 is partly disordered as predicted by simulations, and is positioned to form self-self interactions between symmetry-related molecules. We discuss the importance of RTA loop 34 to 55 as a nucleus for unfolding and aggregation, and draw conclusions for ongoing structure-based minimalist design of RTA-based immunogens.

-	~~{{STRUCTURE_3lc9\| PDB=3lc9 \| SCENE= }}~~	+	Introduction of a disulfide bond leads to stabilization and crystallization of a ricin immunogen.,Compton JR, Legler PM, Clingan BV, Olson MA, Millard CB Proteins. 2011 Apr;79(4):1048-60. doi: 10.1002/prot.22933. Epub 2011 Jan, 5. PMID:21387408<ref>PMID:21387408</ref>

-	~~===Ricin A-chain variant 1-33~~/~~44-198 with engineered disulfide bond===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21387408}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3lc9]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Ricinus_communis Ricinus communis]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA].~~	+

	==See Also==		==See Also==
	*[[Ricin\|Ricin]]		*[[Ricin\|Ricin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:021387408<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Ricinus communis]]		[[Category: Ricinus communis]]
	[[Category: RRNA N-glycosylase]]		[[Category: RRNA N-glycosylase]]
-	[[Category: Compton, J R.]]	+	[[Category: Compton, J R]]
-	[[Category: Legler, P M.]]	+	[[Category: Legler, P M]]
-	[[Category: Millard, C B.]]	+	[[Category: Millard, C B]]
	[[Category: Disulfide bond]]		[[Category: Disulfide bond]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 12:42, 20 October 2012

2012-10-20T12:42:44Z

←Older revision		Revision as of 12:42, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3lc9]] is a 1 chain structure ~~of [[Ricin]]~~ with sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA].	+	[[3lc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA].

	==See Also==		==See Also==

OCA at 09:37, 26 July 2012

2012-07-26T09:37:07Z

←Older revision		Revision as of 09:37, 26 July 2012
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	[[Image:3lc9.png\|left\|200px]]		[[Image:3lc9.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_3lc9\| PDB=3lc9 \| SCENE= }}		{{STRUCTURE_3lc9\| PDB=3lc9 \| SCENE= }}

	===Ricin A-chain variant 1-33/44-198 with engineered disulfide bond===		===Ricin A-chain variant 1-33/44-198 with engineered disulfide bond===

-
-	<!--
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	==See Also==		==See Also==
-	*[[Ricin]]	+	*[[Ricin\|Ricin]]

	==Reference==		==Reference==

OCA: Protected "3lc9" [edit=sysop:move=sysop]

2012-01-25T05:45:06Z

Protected "3lc9" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:45, 25 January 2012

OCA at 05:45, 25 January 2012

2012-01-25T05:45:03Z

←Older revision		Revision as of 05:45, 25 January 2012
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-	~~{{Seed}}~~	+	[[Image:3lc9.png\|left\|200px]]
-	[[Image:3lc9.~~jpg~~\|left\|200px]]	+

	<!--		<!--
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	===Ricin A-chain variant 1-33/44-198 with engineered disulfide bond===		===Ricin A-chain variant 1-33/44-198 with engineered disulfide bond===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21387408}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21387408 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21387408}}

	==About this Structure==		==About this Structure==
-	~~3LC9~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA].	+	[[3lc9]] is a 1 chain structure of [[Ricin]] with sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC9 OCA].
		+
		+	==See Also==
		+	*[[Ricin]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021387408</ref><references group="xtra"/>
	[[Category: Ricinus communis]]		[[Category: Ricinus communis]]
	[[Category: RRNA N-glycosylase]]		[[Category: RRNA N-glycosylase]]
Line 28:		Line 39:
	[[Category: Ricin]]		[[Category: Ricin]]
	[[Category: Toxin]]		[[Category: Toxin]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 10 06:48:11 2010''