2a78
From Proteopedia
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| - | [[Image:2a78.gif|left|200px]] | + | [[Image:2a78.gif|left|200px]] |
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| - | '''Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme''' | + | {{Structure |
| + | |PDB= 2a78 |SIZE=350|CAPTION= <scene name='initialview01'>2a78</scene>, resolution 1.810Å | ||
| + | |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 [ | + | 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:// | + | 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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:46:13 2008'' |
Revision as of 13:46, 20 March 2008
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| , 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
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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