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PDBsum entry 3q9o

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protein ligands links
Transferase PDB id
3q9o
Jmol
Contents
Protein chain
605 a.a.
Ligands
NAD
GOL ×3
Waters ×403
PDB id:
3q9o
Name: Transferase
Title: Full-length cholix toxin from vibrio cholerae in complex wit
Structure: Exotoxin a. Chain: a. Fragment: unp residues 33-666. Synonym: cholix toxin. Engineered: yes
Source: Vibrio cholerae. Organism_taxid: 666. Strain: tp. Gene: chxa, toxa. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.79Å     R-factor:   0.165     R-free:   0.203
Authors: A.R.Merrill,R.Jorgensen,R.J.Fieldhouse
Key ref: R.J.Fieldhouse et al. (2012). The 1.8 Å cholix toxin crystal structure in complex with NAD+ and evidence for a new kinetic model. J Biol Chem, 287, 21176-21188. PubMed id: 22535961
Date:
09-Jan-11     Release date:   04-Jan-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q5EK40  (CHXA_VIBCL) -  Cholix toxin
Seq:
Struc:
 
Seq:
Struc:
666 a.a.
605 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.4.2.36  - NAD(+)--diphthamide ADP-ribosyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: NAD+ + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
NAD(+)
Bound ligand (Het Group name = NAD)
corresponds exactly
+ diphthamide-[translation elongation factor 2]
= nicotinamide
+ N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     3 terms  

 

 
    Added reference    
 
 
J Biol Chem 287:21176-21188 (2012)
PubMed id: 22535961  
 
 
The 1.8 Å cholix toxin crystal structure in complex with NAD+ and evidence for a new kinetic model.
R.J.Fieldhouse, R.Jørgensen, M.R.Lugo, A.R.Merrill.
 
  ABSTRACT  
 
No abstract given.