Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
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...
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Published in | Nature (London) Vol. 415; no. 6870; pp. 396 - 402 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing
24.01.2002
Nature Publishing Group |
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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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AbstractList | 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. 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 angstrom translation and a 30 degree 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. 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, 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[variant prime]-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 [Angstrom] translation and a 30' 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. |
Audience | Academic |
Author | Yan, Shui-Zhong Shen, Yue-Quan Bohm, Andrew Grabarek, Zenon Drum, Chester L Lu, Dan Soelaiman, Sandriyana Tang, Wei-Jen Bard, Joel |
Author_xml | – sequence: 1 givenname: Wei-Jen surname: Tang fullname: Tang, Wei-Jen organization: Ben-May Institute for Cancer Research, The University of Chicago Committee on Neurobiology, The University of Chicago – sequence: 2 givenname: Chester L surname: Drum fullname: Drum, Chester L organization: Ben-May Institute for Cancer Research, The University of Chicago Committee on Neurobiology, The University of Chicago Boston Biomedical Research Institute – sequence: 3 givenname: Shui-Zhong surname: Yan fullname: Yan, Shui-Zhong organization: Ben-May Institute for Cancer Research, The University of Chicago – sequence: 4 givenname: Joel surname: Bard fullname: Bard, Joel organization: Boston Biomedical Research Institute – sequence: 5 givenname: Yue-Quan surname: Shen fullname: Shen, Yue-Quan organization: Ben-May Institute for Cancer Research, The University of Chicago – sequence: 6 givenname: Dan surname: Lu fullname: Lu, Dan organization: Ben-May Institute for Cancer Research, The University of Chicago – sequence: 7 givenname: Sandriyana surname: Soelaiman fullname: Soelaiman, Sandriyana organization: Ben-May Institute for Cancer Research, The University of Chicago – sequence: 8 givenname: Zenon surname: Grabarek fullname: Grabarek, Zenon organization: Boston Biomedical Research Institute – sequence: 9 givenname: Andrew surname: Bohm fullname: Bohm, Andrew organization: Boston Biomedical Research Institute Tufts University School of Medicine |
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ContentType | Journal Article |
Copyright | 2002 INIST-CNRS COPYRIGHT 2002 Nature Publishing Group Copyright Macmillan Journals Ltd. Jan 24, 2002 |
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Keywords | Bacillus anthracis Calcium Enzyme Phosphorus-oxygen lyases Lyases Activation Bacillaceae Binding protein Adenylate cyclase Toxin Bacillales Bacteria Property structure relationship Calmodulin |
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Snippet | 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... |
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SubjectTerms | Adenylyl Cyclases - chemistry Adenylyl Cyclases - metabolism Amino Acid Sequence Animals Anthrax Antigens, Bacterial Bacillus anthracis Bacillus anthracis - enzymology Bacterial Toxins Bacteriology Biological and medical sciences Calmodulin - chemistry Calmodulin - pharmacology Catalysis Catalytic Domain Crystallography, X-Ray edema factor Enzyme Activation Exotoxins - chemistry Exotoxins - metabolism Fundamental and applied biological sciences. Psychology Humans Ions Macromolecular Substances Mammals Metal ions Microbiology Models, Molecular Molecular Sequence Data Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Peptides Protein Binding Protein Conformation Proteins Structure-Activity Relationship Toxicity X-rays |
Title | Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin |
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