› 5cvw

X-ray diffraction
1.25Å resolution

CRYSTAL STRUCTURE OF RTX DOMAIN BLOCK V OF ADENYLATE CYCLASE TOXIN FROM BORDETELLA PERTUSSIS

Released:
DOI: 10.2210/pdb5cvw/pdb
PDB entry 5cvw coloured by chain, front view.
PDB entry 5cvw coloured by chain, side view.
PDB entry 5cvw coloured by chain, top view.
Source organism: Bordetella pertussis 18323
Primary publication:
Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts.
Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P
Mol Cell 62 47-62 (2016)
PMID: 27058787

Function and Biology Details

Reaction catalysed: 
ATP = 3',5'-cyclic AMP + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemolysin Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.02 KDa
Source organism: Bordetella pertussis 18323
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: J7QLC0 (Residues: 1529-1681; Coverage: 9%)
Gene names: BN118_0468, cya, cyaA
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand CA 8 x CA
Ligand EDO 4 x EDO
Ligand GOL 1 x GOL
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: I222
Unit cell:
a: 62.824Å b: 62.983Å c: 77.627Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.139 0.166
Expression system: Escherichia coli BL21(DE3)

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Citations

16 review citations

Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes.
Novak et al. (2017)
15 more

6 mentions without citation

Calcium-Binding Proteins with Disordered Structure and Their Role in Secretion, Storage, and Cellular Signaling.
Grzybowska EA. (2018)
5 more