1dm0

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<StructureSection load='1dm0' size='340' side='right'caption='[[1dm0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1dm0' size='340' side='right'caption='[[1dm0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1dm0]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_dysenteriae"_shiga_1898 "bacillus dysenteriae" shiga 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DM0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1dm0]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_dysenteriae Shigella dysenteriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DM0 FirstGlance]. <br>
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</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>
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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]] 2.5&#8491;</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=1dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dm0 OCA], [https://pdbe.org/1dm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1dm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dm0 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=1dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dm0 OCA], [https://pdbe.org/1dm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1dm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dm0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/STXB_SHIDY STXB_SHIDY]] The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli.<ref>PMID:2677606</ref>
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[https://www.uniprot.org/uniprot/STXA_SHIDY STXA_SHIDY] The A subunit is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits. After endocytosis, the A subunit is cleaved by furin in two fragments, A1 and A2: A1 is the catalytically active fragment, and A2 is essential for holotoxin assembly with the B subunits.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dm0 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dm0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Shigella dysenteriae is the pathogen responsible for the severe form of dysentery in humans. It produces Shiga toxin, the prototype of a family of closely related bacterial protein toxins. We have determined the structure of the holotoxin, an AB5 hexamer, by X-ray crystallography. The five B subunits form a pentameric ring, encircling a helix at the carboxy terminus of the A subunit. The A subunit interacts with the B pentamer via this C-terminal helix and a four-stranded mixed beta-sheet. The fold of the rest of the A subunit is similar to that of the A chain of the plant toxin ricin; both are N-glycosidases. However, the active site in the bacterial holotoxin is blocked by a segment of polypeptide chain. These residues of the A subunit would be released as part of the activation mechanism of the toxin.
 
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Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution.,Fraser ME, Chernaia MM, Kozlov YV, James MN Nat Struct Biol. 1994 Jan;1(1):59-64. PMID:7656009<ref>PMID:7656009</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 1dm0" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Shiga toxin|Shiga toxin]]
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*[[Shiga toxin 3D structures|Shiga toxin 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus dysenteriae shiga 1898]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: RRNA N-glycosylase]]
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[[Category: Shigella dysenteriae]]
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[[Category: Chernaia, M M]]
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[[Category: Chernaia MM]]
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[[Category: Fraser, M E]]
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[[Category: Fraser ME]]
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[[Category: James, M N]]
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[[Category: James MN]]
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[[Category: Kozlov, Y V]]
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[[Category: Kozlov YV]]
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[[Category: Ab5 structure]]
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[[Category: Active site]]
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[[Category: Blocking]]
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[[Category: Polypeptide some]]
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[[Category: Toxin]]
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Revision as of 09:51, 20 March 2024

SHIGA TOXIN

PDB ID 1dm0

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