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Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin

Drum, Chester L., Yan, Shui-Zhong, Bard, Joel, Shen, Yue-Quan, Lu, Dan, Soelaiman, Sandriyana, Grabarek, Zenon, Bohm, Andrew, Tang, Wei-Jen·2002·Nature

DOI 10.1038/415396a

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Abstract

Oedema factor, a calmodulin-activated adenylyl cyclase, is important in the pathogenesis of anthrax. Here we report the X-ray structures of oedema factor with and without bound calmodulin. Oedema factor shares no significant structural homology with mammalian adenylyl cyclases or other proteins. In the active site, 3'-deoxy-ATP and a single metal ion are well positioned for catalysis with histidine 351 as the catalytic base. This mechanism differs from the mechanism of two-metal-ion catalysis proposed for mammalian adenylyl cyclases. Four discrete regions of oedema factor form a surface that recognizes an extended conformation of calmodulin, which is very different from the collapsed conformation observed in other structures of calmodulin bound to effector peptides. On calmodulin binding, an oedema factor helical domain of relative molecular mass 15,000 undergoes a 15 A translation and a 30 degrees rotation away from the oedema factor catalytic core, which stabilizes a disordered loop and leads to enzyme activation. These allosteric changes provide the first molecular details of how calmodulin modulates one of its targets.

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Authors: Drum, C. L., Yan, S.-Z., Bard, J., Shen, Y.-Q., Lu, D., Soelaiman, S., Grabarek, Z., Bohm, A., & Tang, W.-J.
Affiliations: University of Chicago (US)
Boston Biomedical Research Institute (US)
Tufts University (US)
Corresponding author: Tang, Wei-Jen
ORCID: Drum, Chester L.
Grabarek, Zenon
Bohm, Andrew
Tang, Wei-Jen
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2002-01
Volume: 415
Issue: 6870
Pages: 396-402
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/415396a
OpenAlex: W2096942328
Cited by: 413
References: 51
Citations by year: 2025: 4 · 2024: 5 · 2023: 10 · 2022: 11 · 2021: 6 · 2020: 13 · 2019: 12 · 2018: 8 · 2017: 11 · 2016: 12 · 2015: 13 · 2014: 12 · 2013: 14 · 2012: 19
FWCI: 12.98
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: American Cancer Society
American Heart Association
National Institutes of Health
National Institute on Drug Abuse
National Institute of General Medical Sciences
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacillus and Francisella bacterial research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: anthrax toxin, adenylate cyclase, calmodulin, enzyme activation, allosteric regulation, calmodulin binding site, metal ion catalysis, protein structure
MeSH terms: Adenylyl Cyclases, Amino Acid Sequence, Animals, Antigens, Bacterial, Bacillus anthracis, Bacterial Toxins, Calmodulin, Enzyme Activation, Exotoxins, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Structure-Activity Relationship, Crystallography, X-Ray, Catalytic Domain, Macromolecular Substances

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Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin

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