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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5737
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pubmed:dateCreated |
2005-8-15
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pubmed:databankReference |
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pubmed:abstractText |
The Vibrio cholerae bacterium causes devastating diarrhea when it infects the human intestine. The key event is adenosine diphosphate (ADP)-ribosylation of the human signaling protein GSalpha, catalyzed by the cholera toxin A1 subunit (CTA1). This reaction is allosterically activated by human ADP-ribosylation factors (ARFs), a family of essential and ubiquitous G proteins. Crystal structures of a CTA1:ARF6-GTP (guanosine triphosphate) complex reveal that binding of the human activator elicits dramatic changes in CTA1 loop regions that allow nicotinamide adenine dinucleotide (NAD+) to bind to the active site. The extensive toxin:ARF-GTP interface surface mimics ARF-GTP recognition of normal cellular protein partners, which suggests that the toxin has evolved to exploit promiscuous binding properties of ARFs.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
309
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1093-6
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16099990-ADP-Ribosylation Factors,
pubmed-meshheading:16099990-Amino Acid Sequence,
pubmed-meshheading:16099990-Binding Sites,
pubmed-meshheading:16099990-Cholera Toxin,
pubmed-meshheading:16099990-Crystallography, X-Ray,
pubmed-meshheading:16099990-Dimerization,
pubmed-meshheading:16099990-Evolution, Molecular,
pubmed-meshheading:16099990-Guanosine Diphosphate,
pubmed-meshheading:16099990-Guanosine Triphosphate,
pubmed-meshheading:16099990-Humans,
pubmed-meshheading:16099990-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:16099990-Models, Molecular,
pubmed-meshheading:16099990-Molecular Sequence Data,
pubmed-meshheading:16099990-NAD,
pubmed-meshheading:16099990-Protein Binding,
pubmed-meshheading:16099990-Protein Conformation,
pubmed-meshheading:16099990-Protein Structure, Secondary
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pubmed:year |
2005
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pubmed:articleTitle |
Structural basis for the activation of cholera toxin by human ARF6-GTP.
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pubmed:affiliation |
Department of Chemistry, University of Washington, Seattle, WA 98195, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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