2a5g

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(New page: 200px<br /> <applet load="2a5g" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a5g, resolution 2.66&Aring;" /> '''Cholera toxin A1 su...)
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[[Image:2a5g.gif|left|200px]]<br />
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[[Image:2a5g.gif|left|200px]]<br /><applet load="2a5g" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2a5g" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2a5g, resolution 2.66&Aring;" />
caption="2a5g, resolution 2.66&Aring;" />
'''Cholera toxin A1 subunit bound to ARF6(Q67L)'''<br />
'''Cholera toxin A1 subunit bound to ARF6(Q67L)'''<br />
==Overview==
==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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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==
==About this Structure==
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2A5G is a [http://en.wikipedia.org/wiki/Protein_complex 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] with MG, NA and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A5G OCA].
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2A5G is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5G OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Vibrio cholerae]]
[[Category: Vibrio cholerae]]
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[[Category: Hol, W.G.J.]]
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[[Category: Hol, W G.J.]]
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[[Category: Holmes, R.K.]]
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[[Category: Holmes, R K.]]
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[[Category: Jobling, M.G.]]
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[[Category: Jobling, M G.]]
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[[Category: Neal, C.J.O.]]
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[[Category: Neal, C J.O.]]
[[Category: GTP]]
[[Category: GTP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: protein transport/transferase]]
[[Category: protein transport/transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:46:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:46 2008''

Revision as of 14:23, 21 February 2008


2a5g, resolution 2.66Å

Drag the structure with the mouse to rotate

Cholera toxin A1 subunit bound to ARF6(Q67L)

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

2A5G is a Protein complex structure of sequences from Homo sapiens and Vibrio cholerae with , and as ligands. Active as NAD(+)--diphthamide ADP-ribosyltransferase, with EC number 2.4.2.36 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

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