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The structure of the anthrax edema factor (EF) exotoxin reveals evidence of a new adenylate kinase mechanism and the first structure of an active calmodulin-dependent enzyme in complex with calmodulin (CaM). The CaM-free toxin opens to enfold CaM in a way that positions critical EF substrate-binding...

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Veröffentlicht in:	Nature Structural Biology 2002-03, Vol.9 (3), p.156-158
Hauptverfasser:	Meador, William E., Quiocho, Florante A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Adenylyl Cyclases - chemistry Adenylyl Cyclases - metabolism Antigens, Bacterial Bacillus anthracis - chemistry Bacillus anthracis - enzymology Bacillus anthracis - pathogenicity Bacterial Toxins Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Calmodulin - chemistry Calmodulin - metabolism Exotoxins - chemistry Exotoxins - metabolism Life Sciences Membrane Biology Models, Molecular news-and-views Protein Structure Protein Structure, Tertiary
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Beschreibung
Zusammenfassung:	The structure of the anthrax edema factor (EF) exotoxin reveals evidence of a new adenylate kinase mechanism and the first structure of an active calmodulin-dependent enzyme in complex with calmodulin (CaM). The CaM-free toxin opens to enfold CaM in a way that positions critical EF substrate-binding residues near the catalytic site.
ISSN:	1072-8368 1545-9993 1545-9985
DOI:	10.1038/nsb0302-156