2a78

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|PDB= 2a78 |SIZE=350|CAPTION= <scene name='initialview01'>2a78</scene>, resolution 1.810&Aring;
|PDB= 2a78 |SIZE=350|CAPTION= <scene name='initialview01'>2a78</scene>, resolution 1.810&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
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|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|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])
|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])
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|DOMAIN=
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|RELATEDENTRY=[[1u8y|1u8y]], [[1u8z|1u8z]], [[1u90|1u90]], [[1uad|1uad]], [[2bov|2bov]], [[1g24|1G24]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a78 OCA], [http://www.ebi.ac.uk/pdbsum/2a78 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a78 RCSB]</span>
}}
}}
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[[Category: Trankle, J.]]
[[Category: Trankle, J.]]
[[Category: Vogelsgesang, M.]]
[[Category: Vogelsgesang, M.]]
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[[Category: GDP]]
 
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[[Category: MG]]
 
[[Category: bacterial adp-ribosyltransferase]]
[[Category: bacterial adp-ribosyltransferase]]
[[Category: exoenzyme c3]]
[[Category: exoenzyme c3]]
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[[Category: rho]]
[[Category: rho]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:35:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:48:45 2008''

Revision as of 22:48, 30 March 2008


PDB ID 2a78

Drag the structure with the mouse to rotate
, resolution 1.810Å
Ligands: ,
Gene: RALA, RAL (Homo sapiens), C3 (Clostridium botulinum D phage)
Related: 1u8y, 1u8z, 1u90, 1uad, 2bov, 1G24


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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 Structure

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

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:16177825

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