2a78: Difference between revisions

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[[Image:2a78.gif|left|200px]]<br /><applet load="2a78" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2a78.gif|left|200px]]
caption="2a78, resolution 1.810&Aring;" />
 
'''Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme'''<br />
{{Structure
|PDB= 2a78 |SIZE=350|CAPTION= <scene name='initialview01'>2a78</scene>, resolution 1.810&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>
|ACTIVITY=
|GENE= RALA, RAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), C3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29342 Clostridium botulinum D phage])
}}
 
'''Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2A78 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_botulinum_d_phage Clostridium botulinum d phage] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A78 OCA].  
2A78 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_botulinum_d_phage Clostridium botulinum d phage] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A78 OCA].  


==Reference==
==Reference==
Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme., Pautsch A, Vogelsgesang M, Trankle J, Herrmann C, Aktories K, EMBO J. 2005 Oct 19;24(20):3670-80. Epub 2005 Sep 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16177825 16177825]
Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme., Pautsch A, Vogelsgesang M, Trankle J, Herrmann C, Aktories K, EMBO J. 2005 Oct 19;24(20):3670-80. Epub 2005 Sep 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16177825 16177825]
[[Category: Clostridium botulinum d phage]]
[[Category: Clostridium botulinum d phage]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: rho]]
[[Category: rho]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:16 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:46:13 2008''

Revision as of 16:46, 20 March 2008

File:2a78.gif


PDB ID 2a78

Drag the structure with the mouse to rotate
, resolution 1.810Å
Ligands: and
Gene: RALA, RAL (Homo sapiens), C3 (Clostridium botulinum D phage)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme


OverviewOverview

C3 exoenzymes from bacterial pathogens ADP-ribosylate and inactivate low-molecular-mass GTPases of the Rho subfamily. Ral, a Ras subfamily GTPase, binds the C3 exoenzymes from Clostridium botulinum and C. limosum with high affinity without being a substrate for ADP ribosylation. In the complex, the ADP-ribosyltransferase activity of C3 is blocked, while binding of NAD and NAD-glycohydrolase activity remain. Here we report the crystal structure of C3 from C. botulinum in a complex with GDP-bound RalA at 1.8 A resolution. C3 binds RalA with a helix-loop-helix motif that is adjacent to the active site. A quaternary complex with NAD suggests a mode for ADP-ribosyltransferase inhibition. Interaction of C3 with RalA occurs at a unique interface formed by the switch-II region, helix alpha3 and the P loop of the GTPase. C3-binding stabilizes the GDP-bound conformation of RalA and blocks nucleotide release. Our data indicate that C. botulinum exoenzyme C3 is a single-domain toxin with bifunctional properties targeting Rho GTPases by ADP ribosylation and Ral by a guanine nucleotide dissociation inhibitor-like effect, which blocks nucleotide exchange.

About this StructureAbout this Structure

2A78 is a Protein complex structure of sequences from Clostridium botulinum d phage and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme., Pautsch A, Vogelsgesang M, Trankle J, Herrmann C, Aktories K, EMBO J. 2005 Oct 19;24(20):3670-80. Epub 2005 Sep 22. PMID:16177825

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