3mxg

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<StructureSection load='3mxg' size='340' side='right'caption='[[3mxg]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
<StructureSection load='3mxg' size='340' side='right'caption='[[3mxg]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3mxg]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MXG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3mxg]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MXG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XLS:D-XYLOSE+(LINEAR+FORM)'>XLS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stx2B, L0104 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XLS:D-XYLOSE+(LINEAR+FORM)'>XLS</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=3mxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mxg OCA], [https://pdbe.org/3mxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mxg RCSB], [https://www.ebi.ac.uk/pdbsum/3mxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mxg 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=3mxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mxg OCA], [https://pdbe.org/3mxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mxg RCSB], [https://www.ebi.ac.uk/pdbsum/3mxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mxg ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A7UQX3_ECO57 A7UQX3_ECO57]
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Escherichia coli strain O157:H7 is a major cause of food poisoning that can result in severe diarrhea and, in some cases, renal failure. The pathogenesis of E. coli O157:H7 is in large part due to the production of Shiga toxin (Stx), an AB(5) toxin that consists of a ribosomal RNA-cleaving A-subunit surrounded by a pentamer of receptor-binding B subunits. There are two major isoforms, Stx1 and Stx2, which differ dramatically in potency despite having 57% sequence identity. Animal studies and epidemiological studies show Stx2 is associated with more severe disease. Although the molecular basis of this difference is unknown, data suggest it is associated with the B-subunit. Mass spectrometry studies have suggested differential B-pentamer stability between Stx1 and Stx2. We have examined the relative stability of the B-pentamers in solution. Analytical ultracentrifugation using purified B-subunits demonstrates that Stx2B, the more deadly isoform, shows decreased pentamer stability compared to Stx1B (EC(50) = 2.3 microM vs. EC(50) = 0.043 microM for Stx1B). X-ray crystal structures of Stx1B and Stx2B identified a glutamine in Stx2 (versus leucine in Stx1) within the otherwise strongly hydrophobic interface between B-subunits. Interchanging these residues switches the stability phenotype of the B-pentamers of Stx1 and Stx2, as demonstrated by analytical ultracentrifugation and circular dichroism. These studies demonstrate a profound difference in stability of the B-pentamers in Stx1 and Stx2, illustrate the mechanistic basis for this differential stability, and provide novel reagents to test the basis for differential pathogenicity of these toxins.
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Molecular basis of differential B-pentamer stability of Shiga toxins 1 and 2.,Conrady DG, Flagler MJ, Friedmann DR, Vander Wielen BD, Kovall RA, Weiss AA, Herr AB PLoS One. 2010 Dec 28;5(12):e15153. PMID:21203383<ref>PMID:21203383</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3mxg" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Shiga toxin 3D structures|Shiga toxin 3D structures]]
*[[Shiga toxin 3D structures|Shiga toxin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eco57]]
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[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Flagler, M J]]
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[[Category: Flagler MJ]]
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[[Category: Friedmann, D R]]
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[[Category: Friedmann DR]]
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[[Category: Kovall, R A]]
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[[Category: Kovall RA]]
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[[Category: Wielen, B D.Vander]]
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[[Category: Vander Wielen BD]]
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[[Category: Shiga toxin]]
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[[Category: Stx2b pentamer]]
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[[Category: Toxin]]
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Revision as of 09:58, 14 February 2024

Structure of Shiga Toxin type 2 (Stx2) B Pentamer Mutant Q40L

PDB ID 3mxg

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