1lvc

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1lvc, resolution 3.60Å ()

Ligands:

, ,

Activity:

Adenylate cyclase, with EC number 4.6.1.1

Related:

1k90

Structural annotation:
Resources:	CATH : 1Lvcd01, 1Lvcd02, 1Lvce01, 1Lvce02, 1Lvcf02, 1Lvcf01 InterPro : Ipr014781, Ipr005165, Ipr003541 Pfam : PF03497 SCOP : d1lvca_, d1lvcb_, d1lvcc_ UniProt : P40136, P62158

Functional annotation:
Cellular component:	extracellular region
Biological process:	pathogenesis cAMP biosynthetic process
Molecular function:	protein binding ATP binding adenylate cyclase activity catalytic activity lyase activity metal ion binding magnesium ion binding calcium- and calmodulin-responsive adenylate cyclase activity calcium ion binding calmodulin binding nucleotide binding

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin and 2' deoxy, 3' anthraniloyl ATPCrystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin and 2' deoxy, 3' anthraniloyl ATP

Publication Abstract from PubMed

Edema factor (EF) and CyaA are calmodulin (CaM)-activated adenylyl cyclase exotoxins involved in the pathogenesis of anthrax and whooping cough, respectively. Using spectroscopic, enzyme kinetic and surface plasmon resonance spectroscopy analyses, we show that low Ca(2+) concentrations increase the affinity of CaM for EF and CyaA causing their activation, but higher Ca(2+) concentrations directly inhibit catalysis. Both events occur in a physiologically relevant range of Ca(2+) concentrations. Despite the similarity in Ca(2+) sensitivity, EF and CyaA have substantial differences in CaM binding and activation. CyaA has 100-fold higher affinity for CaM than EF. CaM has N- and C-terminal globular domains, each binding two Ca(2+) ions. CyaA can be fully activated by CaM mutants with one defective C-terminal Ca(2+)-binding site or by either terminal domain of CaM while EF cannot. EF consists of a catalytic core and a helical domain, and both are required for CaM activation of EF. Mutations that decrease the interaction of the helical domain with the catalytic core create an enzyme with higher sensitivity to Ca(2+)-CaM activation. However, CyaA is fully activated by CaM without the domain corresponding to the helical domain of EF.

Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins., Shen Y, Lee YS, Soelaiman S, Bergson P, Lu D, Chen A, Beckingham K, Grabarek Z, Mrksich M, Tang WJ, EMBO J. 2002 Dec 16;21(24):6721-32. PMID:12485993

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this StructureAbout this Structure

1LVC is a 6 chains structure of sequences from Bacillus anthracis and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Shen Y, Lee YS, Soelaiman S, Bergson P, Lu D, Chen A, Beckingham K, Grabarek Z, Mrksich M, Tang WJ. Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins. EMBO J. 2002 Dec 16;21(24):6721-32. PMID:12485993

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OCA

[1] Shen Y, Lee YS, Soelaiman S, Bergson P, Lu D, Chen A, Beckingham K, Grabarek Z, Mrksich M, Tang WJ. Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins. EMBO J. 2002 Dec 16;21(24):6721-32. PMID:12485993

[xtra 1]