1Y0V Lyase date Nov 16, 2004
title Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate
authors Y.Shen, N.L.Zhukovskaya, Q.Guo, J.Florian, W.-J.Tang
compound source
Molecule: Calmodulin-Sensitive Adenylate Cyclase
Chain: A, B, C, D, E, F
Synonym: Atp Pyrophosphate-Lyase, Adenylyl Cyclase, Edema Factor, Ef, Anthrax Edema Toxin Adenylate Cyclase Component;
Ec: 4.6.1.1
Engineered: Yes
Organism_scientific: Bacillus Anthracis
Gene: Cya
Expression_system: Eschericia Coli
Expression_system_common: Bacteria
Expression_system_strain: Bl21
Expression_system_vector_type: Plasmid

Molecule: Calmodulin
Chain: H, I, J, K, L, M
Synonym: Cam
Engineered: Yes

Organism_scientific: Xenopus Laevis
Organism_common: African Clawed Frog
Gene: Calm1
Expression_system: Eschericia Coli
Expression_system_common: Bacteria
Expression_system_strain: Bl21
Expression_system_vector_type: Plasmid
symmetry Space Group: C 1 2 1
R_factor 0.286
crystal
cell
length a length b length c angle alpha angle beta angle gamma
317.509 183.348 141.812 90.00 90.05 90.00
method X-Ray Diffractionresolution 3.60 Å
ligand CA, MG, POP enzyme Adenylate cyclase;. Adenylylcyclase;. Adenyl cyclase;. 3',5'-cyclic AMP synthetase. Lyase E.C.4.6.1.1 BRENDA
domain The metal ion is coordinated by residues from ca; calmodulin probably binds in a multistep fashion first to residues in ca and then to residues present in the linker and the helical domain. The pa-binding region is found in both b.anthracis ef and lf. The c-terminal region contains the calmodulin-dependent activation domain and the catalytic site. This region is composed of three globular domains: ca, cb and a helical domain connected to ca by a linker. The n-terminal region contains the residues responsible for binding to pa63. The active site lies at the interface of ca and cb.
similarity Contains 4 ef-hand domains. Belongs to the adenylyl cyclase class-2 family.[Anthrax_toxA]
subunit Ef probably forms oligomers as part of the translocation machinery, formed by an heterocomplex of pa63 monomers and ef subunits, and it is functional as a monomer in the host cell. Anthrax toxins are composed of three distinct proteins, a protective antigen (pa), a lethal factor (lf) and an edema factor (ef). None of these is toxic by itself. Pa+lf forms the lethal toxin (letx); pa+ef forms the edema toxin (edtx).
catalytic activ. Atp = 3',5'-cyclic amp + diphosphate.
subcellular loc. Secreted protein.
enzyme regulation It has an absolute requirement for host calmodulin for its activation. Inhibited by ethyl 5- aminopyrazolo[1,5-a]quinazoline-3-carboxylate.
genes BXA0141, GBAA, cya (B. anthracis); cya (B. pertussis); GNAS (B. taurus); ADCY5 (C. familiaris); CAMC, CAMIII, CALM3 (H. sapiens); MT1302 (M. tuberculosis); Adcy2 (R. norvegicus); 4.1, 4.3, GRESAG (T. brucei); calm2 (X. laevis)
function One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. Among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases. Ef is a calmodulin-dependent adenylyl cyclase that, when associated with pa, causes edema. Ef is not toxic by itself and it is required for the survival of germinated spores within macrophages at the early stages of infection. Calmodulin mediates the control of a large number of enzymes by ca(2+). Provokes dramatic elevation of intracellular camp levels in the host.
Gene
Ontology
ChainFunctionProcessComponent
F, A, E, B, C, D
  • nucleotide binding
  • magnesium ion binding
  • adenylate cyclase activity
  • calcium ion binding
  • protein binding
  • calmodulin binding
  • ATP binding
  • lyase activity
  • metal ion binding
  • cAMP biosynthetic process
  • pathogenesis
  • extracellular region
  • J, K, H, M, I, L
  • calcium ion binding
  • protein binding
  • G-protein coupled receptor p...
  • cytoplasm
  • plasma membrane
  • disease Calmodulin 3; Calm3
    Primary referenceCalcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor., Shen Y, Zhukovskaya NL, Guo Q, Florian J, Tang WJ, EMBO J 2005 Mar 9;24(5):929-41. Epub 2005 Feb 17. PMID:15719022
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (959 Kb) [Save to disk]
  • Biological Unit Coordinates (1y0v.pdb1.gz) 152 Kb
  • Biological Unit Coordinates (1y0v.pdb2.gz) 151 Kb
  • Biological Unit Coordinates (1y0v.pdb3.gz) 151 Kb
  • Biological Unit Coordinates (1y0v.pdb4.gz) 151 Kb
  • Biological Unit Coordinates (1y0v.pdb5.gz) 151 Kb
  • Biological Unit Coordinates (1y0v.pdb6.gz) 152 Kb
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