2a78
From Proteopedia
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|PDB= 2a78 |SIZE=350|CAPTION= <scene name='initialview01'>2a78</scene>, resolution 1.810Å | |PDB= 2a78 |SIZE=350|CAPTION= <scene name='initialview01'>2a78</scene>, resolution 1.810Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-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]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1u8y|1u8y]], [[1u8z|1u8z]], [[1u90|1u90]], [[1uad|1uad]], [[2bov|2bov]], [[1g24|1G24]] | ||
+ | |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.]] | ||
- | [[Category: GDP]] | ||
- | [[Category: MG]] | ||
[[Category: bacterial adp-ribosyltransferase]] | [[Category: bacterial adp-ribosyltransferase]] | ||
[[Category: exoenzyme c3]] | [[Category: exoenzyme c3]] | ||
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[[Category: rho]] | [[Category: rho]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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, resolution 1.810Å | |||||||
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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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