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Toxin PDB id
2vl8
Jmol
Contents
Protein chains
539 a.a. *
Ligands
UDP ×3
CTS ×3
Metals
_CA ×5
Waters ×400
* Residue conservation analysis
PDB id:
2vl8
Name: Toxin
Title: Crystal structure of the catalytic domain of lethal toxin from clostridium sordellii in complex with udp, castanospermine and calcium ion
Structure: Cytotoxin l. Chain: a, b, c. Fragment: catalytic domain, residues 1-546. Engineered: yes. Mutation: yes
Source: Clostridium sordellii. Organism_taxid: 1505. Strain: 6018. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.31Å     R-factor:   0.218     R-free:   0.255
Authors: T.Jank,M.O.P.Ziegler,G.E.Schulz,K.Aktories
Key ref: T.Jank et al. (2008). Inhibition of the glucosyltransferase activity of clostridial Rho/Ras-glucosylating toxins by castanospermine. Febs Lett, 582, 2277-2282. PubMed id: 18505687 DOI: 10.1016/j.febslet.2008.05.025
Date:
09-Jan-08     Release date:   17-Jun-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q46342  (Q46342_CLOSO) -  Cytotoxin L
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		2364 a.a.
539 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     transferase activity, transferring glycosyl groups     1 term  

 

 
DOI no: 10.1016/j.febslet.2008.05.025 Febs Lett 582:2277-2282 (2008)
PubMed id: 18505687  
 
 
Inhibition of the glucosyltransferase activity of clostridial Rho/Ras-glucosylating toxins by castanospermine.
T.Jank, M.O.Ziegler, G.E.Schulz, K.Aktories.
 
  ABSTRACT  
 
Castanospermine was identified as an inhibitor of the Rho/Ras-glucosylating Clostridium sordellii lethal toxin and Clostridium difficile toxin B. Microinjection of castanospermine into embryonic bovine lung cells prevented the cytotoxic effects of toxins. The crystal structure of the glucosyltransferase domain of C. sordellii lethal toxin in complex with castanospermine, UDP and a calcium ion was solved at a resolution of 2.3A. The inhibitor binds in a conformation that brings its four hydroxyl groups and its N-atom almost exactly in the positions of the four hydroxyls and of the ring oxygen of the glucosyl moiety of UDP-glucose, respectively.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21308451 N.Suwantarat, and D.A.Bobak (2011).
Current Status of Nonantibiotic and Adjunct Therapies for Clostridium difficile Infection.
  Curr Infect Dis Rep, 13, 21-27.  
20714463 D.J.Wardrop, and S.L.Waidyarachchi (2010).
Synthesis and biological activity of naturally occurring α-glucosidase inhibitors.
  Nat Prod Rep, 27, 1431-1468.  
  19340897 P.Hookman, and J.S.Barkin (2009).
Clostridium difficile associated infection, diarrhea and colitis.
  World J Gastroenterol, 15, 1554-1580.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.