2a5g: Difference between revisions

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{{STRUCTURE_2a5g|  PDB=2a5g  |  SCENE=  }}  
{{STRUCTURE_2a5g|  PDB=2a5g  |  SCENE=  }}  


'''Cholera toxin A1 subunit bound to ARF6(Q67L)'''
===Cholera toxin A1 subunit bound to ARF6(Q67L)===




==Overview==
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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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==About this Structure==
==About this Structure==
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[[Category: Neal, C J.O.]]
[[Category: Neal, C J.O.]]
[[Category: Protein transport/transferase]]
[[Category: Protein transport/transferase]]
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Revision as of 10:40, 28 July 2008

File:2a5g.png

Template:STRUCTURE 2a5g

Cholera toxin A1 subunit bound to ARF6(Q67L)Cholera toxin A1 subunit bound to ARF6(Q67L)

Template:ABSTRACT PUBMED 16099990

About this StructureAbout this Structure

2A5G is a Protein complex structure of sequences from Homo sapiens and Vibrio cholerae. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the activation of cholera toxin by human ARF6-GTP., O'Neal CJ, Jobling MG, Holmes RK, Hol WG, Science. 2005 Aug 12;309(5737):1093-6. PMID:16099990

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