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2a78
From Proteopedia
| 2a78, resolution 1.81Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||||
| Ligands: | , | ||||||||
| Gene: | RALA, RAL (Homo sapiens), C3 (Clostridium botulinum D phage) | ||||||||
| Related: | 1u8y, 1u8z, 1u90, 1uad, 2bov, 1g24 | ||||||||
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| 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
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2a78 is a 2 chain structure with sequence from Clostridium botulinum d phage and Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Pautsch A, Vogelsgesang M, Trankle J, Herrmann C, Aktories K. Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme. EMBO J. 2005 Oct 19;24(20):3670-80. Epub 2005 Sep 22. PMID:16177825
- Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR. Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase. Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5357-62. Epub 2005 Apr 4. PMID:15809419
