7rb4 - Revision history

OCA at 09:34, 9 October 2024

2024-10-09T09:34:09Z

← Older revision		Revision as of 09:34, 9 October 2024
Line 3:		Line 3:
	<StructureSection load='7rb4' size='340' side='right'caption='[[7rb4]], [[Resolution\|resolution]] 2.19Å' scene=''>		<StructureSection load='7rb4' size='340' side='right'caption='[[7rb4]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>~~[[7rb4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Seinonella_peptonophila Seinonella peptonophila].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB4 FirstGlance]. <br>		<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB4 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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]] 2.19Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=7rb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb4 OCA], [https://pdbe.org/7rb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb4 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb4 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=7rb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb4 OCA], [https://pdbe.org/7rb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb4 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb4 ProSAT]</span></td></tr>
	</table>		</table>
	~~== Function ==~~
	~~[https://www.uniprot.org/uniprot/A0A1M4ZWA4_9BACL A0A1M4ZWA4_9BACL]~~
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Diphtheria toxin (DT) is the archetype for bacterial exotoxins implicated in human diseases and has played a central role in defining the field of toxinology since its discovery in 1888. Despite being one of the most extensively characterized bacterial toxins, the origins and evolutionary adaptation of DT to human hosts remain unknown. Here, we determined the first high-resolution structures of DT homologs outside of the Corynebacterium genus. DT homologs from Streptomyces albireticuli (17% identity to DT) and Seinonella peptonophila (20% identity to DT), despite showing no toxicity toward human cells, display significant structural similarities to DT sharing both the overall Y-shaped architecture of DT as well as the individual folds of each domain. Through a systematic investigation of individual domains, we show that the functional determinants of host range extend beyond an inability to bind cellular receptors; major differences in pH-induced pore-formation and cytosolic release further dictate the delivery of toxic catalytic moieties into cells, thus providing multiple mechanisms for a conserved structural fold to adapt to different hosts. Our work provides structural insights into the expanding DT family of toxins, and highlights key transitions required for host adaptation.

	Structures of distant diphtheria toxin homologs reveal functional determinants of an evolutionarily conserved toxin scaffold.,Sugiman-Marangos SN, Gill SK, Mansfield MJ, Orrell KE, Doxey AC, Melnyk RA Commun Biol. 2022 Apr 19;5(1):375. doi: 10.1038/s42003-022-03333-9. PMID:35440624<ref>PMID:35440624</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 7rb4" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Seinonella peptonophila]]~~
	[[Category: Gill SK]]		[[Category: Gill SK]]
	[[Category: Melnyk RA]]		[[Category: Melnyk RA]]
	[[Category: Sugiman-Marangos SN]]		[[Category: Sugiman-Marangos SN]]

OCA at 07:33, 3 November 2022

2022-11-03T07:33:24Z

← Older revision		Revision as of 07:33, 3 November 2022
Line 1:		Line 1:

	==Crystal structure of Peptono Toxin, a diphtheria toxin homolog, from Seinonella peptonophila==		==Crystal structure of Peptono Toxin, a diphtheria toxin homolog, from Seinonella peptonophila==
	<StructureSection load='7rb4' size='340' side='right'caption='[[7rb4]]' scene=''>		<StructureSection load='7rb4' size='340' side='right'caption='[[7rb4]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[7rb4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Seinonella_peptonophila Seinonella peptonophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB4 FirstGlance]. <br>
	</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=7rb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb4 OCA], [https://pdbe.org/7rb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb4 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb4 ProSAT]</span></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=7rb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb4 OCA], [https://pdbe.org/7rb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb4 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb4 ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/A0A1M4ZWA4_9BACL A0A1M4ZWA4_9BACL]
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Diphtheria toxin (DT) is the archetype for bacterial exotoxins implicated in human diseases and has played a central role in defining the field of toxinology since its discovery in 1888. Despite being one of the most extensively characterized bacterial toxins, the origins and evolutionary adaptation of DT to human hosts remain unknown. Here, we determined the first high-resolution structures of DT homologs outside of the Corynebacterium genus. DT homologs from Streptomyces albireticuli (17% identity to DT) and Seinonella peptonophila (20% identity to DT), despite showing no toxicity toward human cells, display significant structural similarities to DT sharing both the overall Y-shaped architecture of DT as well as the individual folds of each domain. Through a systematic investigation of individual domains, we show that the functional determinants of host range extend beyond an inability to bind cellular receptors; major differences in pH-induced pore-formation and cytosolic release further dictate the delivery of toxic catalytic moieties into cells, thus providing multiple mechanisms for a conserved structural fold to adapt to different hosts. Our work provides structural insights into the expanding DT family of toxins, and highlights key transitions required for host adaptation.

			Structures of distant diphtheria toxin homologs reveal functional determinants of an evolutionarily conserved toxin scaffold.,Sugiman-Marangos SN, Gill SK, Mansfield MJ, Orrell KE, Doxey AC, Melnyk RA Commun Biol. 2022 Apr 19;5(1):375. doi: 10.1038/s42003-022-03333-9. PMID:35440624<ref>PMID:35440624</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 7rb4" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
			[[Category: Seinonella peptonophila]]
	[[Category: Gill SK]]		[[Category: Gill SK]]
	[[Category: Melnyk RA]]		[[Category: Melnyk RA]]
	[[Category: Sugiman-Marangos SN]]		[[Category: Sugiman-Marangos SN]]

OCA at 02:55, 21 April 2022

2022-04-21T02:55:53Z

← Older revision		Revision as of 02:55, 21 April 2022
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry~~ 7rb4 is ~~ON HOLD until Paper Publication~~		==Crystal structure of Peptono Toxin, a diphtheria toxin homolog, from Seinonella peptonophila==
			<StructureSection load='7rb4' size='340' side='right'caption='[[7rb4]]' scene=''>
	~~Authors~~:		== Structural highlights ==
			<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB4 FirstGlance]. <br>
	~~Description~~:		</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=7rb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb4 OCA], [https://pdbe.org/7rb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb4 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb4 ProSAT]</span></td></tr>
	[[Category: ~~Unreleased Structures~~]]		</table>
			__TOC__
			</StructureSection>
			[[Category: Large Structures]]
			[[Category: Gill SK]]
			[[Category: Melnyk RA]]
			[[Category: Sugiman-Marangos SN]]

OCA: Protected "7rb4" [edit=sysop:move=sysop]

2021-07-14T08:55:28Z

Protected "7rb4" [edit=sysop:move=sysop]

← Older revision	Revision as of 08:55, 14 July 2021
(No difference)

OCA: New page: '''Unreleased structure''' The entry 7rb4 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

2021-07-14T08:55:27Z

New page: '''Unreleased structure''' The entry 7rb4 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7rb4 is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]