3ho6: Difference between revisions

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<StructureSection load='3ho6' size='340' side='right' caption='[[3ho6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3ho6' size='340' side='right' caption='[[3ho6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ho6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/[clostridium]_difficile [clostridium] difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HO6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ho6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HO6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tcdA, toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 [Clostridium] difficile])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tcdA, toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</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=3ho6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ho6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ho6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ho6 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=3ho6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ho6 OCA], [http://pdbe.org/3ho6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ho6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ho6 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TOXA_CLODI TOXA_CLODI]] Only after the enteral delivery of the enterotoxin A may the characteristic disease called pseudomembranous colitis be induced.  
[[http://www.uniprot.org/uniprot/TOXA_PEPDI TOXA_PEPDI]] Only after the enteral delivery of the enterotoxin A may the characteristic disease called pseudomembranous colitis be induced.  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=3ho6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3ho6" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus difficilis hall and o'toole 1935]]
[[Category: Lacy, D B]]
[[Category: Lacy, D B]]
[[Category: Pruitt, R N]]
[[Category: Pruitt, R N]]

Revision as of 12:32, 8 February 2016

Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in clostridium difficile toxin AStructure-function analysis of inositol hexakisphosphate-induced autoprocessing in clostridium difficile toxin A

Structural highlights

3ho6 is a 2 chain structure with sequence from "bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:tcdA, toxA ("Bacillus difficilis" Hall and O'Toole 1935)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TOXA_PEPDI] Only after the enteral delivery of the enterotoxin A may the characteristic disease called pseudomembranous colitis be induced.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The action of Clostridium difficile toxins A and B depends on inactivation of host small G-proteins by glucosylation. Cellular inositol hexakisphosphate (InsP6) induces an autocatalytic cleavage of the toxins, releasing an N-terminal glucosyltransferase domain into the host cell cytosol. We have defined the cysteine protease domain (CPD) responsible for autoprocessing within toxin A (TcdA) and report the 1.6 A x-ray crystal structure of the domain bound to InsP6. InsP6 is bound in a highly basic pocket that is separated from an unusual active site by a beta-flap structure. Functional studies confirm an intramolecular mechanism of cleavage and highlight specific residues required for InsP6-induced TcdA processing. Analysis of the structural and functional data in the context of sequences from similar and diverse origins highlights a C-terminal extension and a pi-cation interaction within the beta-flap that appear to be unique among the large clostridial cytotoxins.

Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in Clostridium difficile toxin A.,Pruitt RN, Chagot B, Cover M, Chazin WJ, Spiller B, Lacy DB J Biol Chem. 2009 Aug 14;284(33):21934-40. Epub 2009 Jun 24. PMID:19553670[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Pruitt RN, Chagot B, Cover M, Chazin WJ, Spiller B, Lacy DB. Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in Clostridium difficile toxin A. J Biol Chem. 2009 Aug 14;284(33):21934-40. Epub 2009 Jun 24. PMID:19553670 doi:10.1074/jbc.M109.018929

3ho6, resolution 1.60Å

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