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http://purl.uniprot.org/citations/15719022http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15719022http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15719022http://www.w3.org/2000/01/rdf-schema#comment"Edema factor (EF), a key anthrax exotoxin, has an anthrax protective antigen-binding domain (PABD) and a calmodulin (CaM)-activated adenylyl cyclase domain. Here, we report the crystal structures of CaM-bound EF, revealing the architecture of EF PABD. CaM has N- and C-terminal domains and each domain can bind two calcium ions. Calcium binding induces the conformational change of CaM from closed to open. Structures of the EF-CaM complex show how EF locks the N-terminal domain of CaM into a closed conformation regardless of its calcium-loading state. This represents a mechanism of how CaM effector alters the calcium affinity of CaM and uncouples the conformational change of CaM from calcium loading. Furthermore, structures of EF-CaM complexed with nucleotides show that EF uses two-metal-ion catalysis, a prevalent mechanism in DNA and RNA polymerases. A histidine (H351) further facilitates the catalysis of EF by activating a water to deprotonate 3'OH of ATP. Mammalian adenylyl cyclases share no structural similarity with EF and they also use two-metal-ion catalysis, suggesting the catalytic mechanism-driven convergent evolution of two structurally diverse adenylyl cyclases."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7600574"xsd:string
http://purl.uniprot.org/citations/15719022http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7600574"xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Tang W.-J."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Tang W.-J."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Guo Q."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Guo Q."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Florian J."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Florian J."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Zhukovskaya N.L."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/author"Zhukovskaya N.L."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/pages"929-941"xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/pages"929-941"xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/title"Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/title"Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor."xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/volume"24"xsd:string
http://purl.uniprot.org/citations/15719022http://purl.uniprot.org/core/volume"24"xsd:string