2a78
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2a78.gif|left|200px]] | [[Image:2a78.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2a78", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2a78| PDB=2a78 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme''' | '''Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme''' | ||
| Line 31: | Line 28: | ||
[[Category: Trankle, J.]] | [[Category: Trankle, J.]] | ||
[[Category: Vogelsgesang, M.]] | [[Category: Vogelsgesang, M.]] | ||
| - | [[Category: | + | [[Category: Bacterial adp-ribosyltransferase]] |
| - | [[Category: | + | [[Category: Exoenzyme c3]] |
| - | [[Category: | + | [[Category: Gdp-binding]] |
| - | [[Category: | + | [[Category: Ral]] |
| - | [[Category: | + | [[Category: Rho]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:41:52 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:41, 3 May 2008
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 Page seeded by OCA on Sat May 3 18:41:52 2008
