X-ray diffraction
2.25Å resolution

Contact-dependent growth inhibition toxin-immunity protein complex from from E. coli 3006, full-length

Source organism: Escherichia coli 3006
Entry authors: Michalska K, Stols L, Eschenfeldt W, Hayes CS, Goulding CW, Joachimiak A, Midwest Center for Structural Genomics (MCSG), Structure-Function Analysis of Polymorphic CDI Toxin-Immunity Protein Complexes (UC4CDI), Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reactions catalysed:
Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
2 glutathione + ROOH = glutathione disulfide + H(2)O + ROH
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
ATP + a protein = ADP + a phosphoprotein
A carboxylic ester + H(2)O = an alcohol + a carboxylate
Release of N-terminal proline from a peptide.
(1a) ATP + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
ATP + H(2)O = ADP + phosphate
Cutin + H(2)O = cutin monomers
(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH
NTP + H(2)O = NDP + phosphate
Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
contact-dependent toxin CdiA Chain: A
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 36.61 KDa
Source organism: Escherichia coli 3006
Expression system: Escherichia coli BL21(DE3)
contact-dependent immunity protein CdiI Chain: I
Molecule details ›
Chain: I
Length: 167 amino acids
Theoretical weight: 19.22 KDa
Source organism: Escherichia coli 3006
Expression system: Escherichia coli BL21(DE3)
  • Canonical: A0A2A2C800 (Residues: 1-161; Coverage: 100%)
Gene names: AW119_27540, BMT50_10330, BTQ06_14240, BvCmsKKP036_01245, BvCmsNSP072_04647, D1H34_005129, DEO04_20970, DEO05_20370, DEO06_21475, DEO07_25860, DEO09_20225, DEO10_20490, DEO11_20380, IAI11_23780

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 41Å b: 71.769Å c: 175.538Å
α: 90° β: 90° γ: 90°
R R work R free
0.185 0.182 0.234
Expression system: Escherichia coli BL21(DE3)