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2a5d
From Proteopedia
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| - | [[Image:2a5d.gif|left|200px]] | + | [[Image:2a5d.gif|left|200px]] |
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| - | '''Structural basis for the activation of cholera toxin by human ARF6-GTP''' | + | {{Structure |
| + | |PDB= 2a5d |SIZE=350|CAPTION= <scene name='initialview01'>2a5d</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GTP:GUANOSINE-5'-TRIPHOSPHATE'>GTP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/NAD(+)--diphthamide_ADP-ribosyltransferase NAD(+)--diphthamide ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.36 2.4.2.36] | ||
| + | |GENE= ARF6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), ctxA, toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 Vibrio cholerae]) | ||
| + | }} | ||
| + | |||
| + | '''Structural basis for the activation of cholera toxin by human ARF6-GTP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2A5D is a [ | + | 2A5D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5D OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16099990 16099990] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: NAD(+)--diphthamide ADP-ribosyltransferase]] | [[Category: NAD(+)--diphthamide ADP-ribosyltransferase]] | ||
| Line 25: | Line 34: | ||
[[Category: protein transport/transferase]] | [[Category: protein transport/transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:45:33 2008'' |
Revision as of 13:45, 20 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | ARF6 (Homo sapiens), ctxA, toxA (Vibrio cholerae) | ||||||
| Activity: | NAD(+)--diphthamide ADP-ribosyltransferase, with EC number 2.4.2.36 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural basis for the activation of cholera toxin by human ARF6-GTP
Overview
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.
About this Structure
2A5D is a Protein complex structure of sequences from Homo sapiens and Vibrio cholerae. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 15:45:33 2008
