› 1s26

X-ray diffraction
3Å resolution

Structure of Anthrax Edema Factor-Calmodulin-alpha,beta-methyleneadenosine 5'-triphosphate Complex Reveals an Alternative Mode of ATP Binding to the Catalytic Site

Released:
DOI: 10.2210/pdb1s26/pdb
PDB entry 1s26 coloured by chain, front view.
PDB entry 1s26 coloured by chain, side view.
PDB entry 1s26 coloured by chain, top view.
Source organisms:
Primary publication:
Structure of anthrax edema factor-calmodulin-adenosine 5'-(alpha,beta-methylene)-triphosphate complex reveals an alternative mode of ATP binding to the catalytic site.
Shen Y, Guo Q, Zhukovskaya NL, Drum CL, Bohm A, Tang WJ
Biochem Biophys Res Commun 317 309-14 (2004)
PMID: 15063758

Function and Biology Details

Reaction catalysed: 
ATP = 3',5'-cyclic AMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-534416 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-sensitive adenylate cyclase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 510 amino acids
Theoretical weight: 58.81 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P40136 (Residues: 291-800; Coverage: 67%)
Gene names: BXA0141, GBAA_pXO1_0142, cya, pXO1-122
Sequence domains:
Structure domains:
Calmodulin-1 Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 148 amino acids
Theoretical weight: 16.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0DP23 (Residues: 2-149; Coverage: 99%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

3 bound ligands:
Ligand YB 3 x YB
Ligand APC 3 x APC
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: I222
Unit cell:
a: 117.555Å b: 167.605Å c: 345.346Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.264 0.264 0.304
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Structural diversity of calmodulin binding to its target sites.
Tidow et al. (2013)
4 more

4 mentions without citation

Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors.
Laine et al. (2012)
3 more