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[[Image:1dm0.gif|left|200px]]
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{{STRUCTURE_1dm0|  PDB=1dm0  |  SCENE=  }}
'''SHIGA TOXIN'''


==SHIGA TOXIN==
<StructureSection load='1dm0' size='340' side='right'caption='[[1dm0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dm/1dm0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1DM0 is a [[Protein complex]] structure of sequences from [http://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].
</div>
<div class="pdbe-citations 1dm0" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/7656009 7656009]
*[[Shiga toxin 3D structures|Shiga toxin 3D structures]]
[[Category: Protein complex]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Shigella dysenteriae]]
[[Category: Shigella dysenteriae]]
[[Category: RRNA N-glycosylase]]
[[Category: Chernaia MM]]
[[Category: Chernaia, M M.]]
[[Category: Fraser ME]]
[[Category: Fraser, M E.]]
[[Category: James MN]]
[[Category: James, M N.]]
[[Category: Kozlov YV]]
[[Category: Kozlov, Y V.]]
[[Category: Ab5 structure]]
[[Category: Active site]]
[[Category: Blocking]]
[[Category: Polypeptide some]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:00:12 2008''

Latest revision as of 04:27, 17 October 2024

SHIGA TOXIN

1dm0, resolution 2.50Å

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