1lvc
From Proteopedia
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===Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin and 2' deoxy, 3' anthraniloyl ATP=== | ===Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin and 2' deoxy, 3' anthraniloyl ATP=== | ||
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{{ABSTRACT_PUBMED_12485993}} | {{ABSTRACT_PUBMED_12485993}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[1lvc]] is a 6 chain structure of [[Adenylyl cyclase]] and [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVC OCA]. | + | [[1lvc]] is a 6 chain structure of [[Adenylyl cyclase]], [[Anthrax edema factor]] and [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVC OCA]. |
==See Also== | ==See Also== | ||
| - | *[[Adenylyl cyclase]] | + | *[[Adenylyl cyclase|Adenylyl cyclase]] |
| - | *[[Calmodulin]] | + | *[[Anthrax edema factor|Anthrax edema factor]] |
| + | *[[Calmodulin|Calmodulin]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:012485993</ref><references group="xtra"/> |
[[Category: Adenylate cyclase]] | [[Category: Adenylate cyclase]] | ||
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
Revision as of 21:15, 26 July 2012
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| 1lvc, resolution 3.60Å () | |||||||||
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| Ligands: | , , | ||||||||
| Activity: | Adenylate cyclase, with EC number 4.6.1.1 | ||||||||
| Related: | 1k90 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin and 2' deoxy, 3' anthraniloyl ATP
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 Structure
1lvc is a 6 chain structure of Adenylyl cyclase, Anthrax edema factor and Calmodulin with sequence from Bacillus anthracis and Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- 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
