2a78

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{{STRUCTURE_2a78| PDB=2a78 | SCENE= }}
{{STRUCTURE_2a78| PDB=2a78 | SCENE= }}
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'''Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme'''
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===Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16177825}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16177825 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16177825}}
==About this Structure==
==About this Structure==
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==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://www.ncbi.nlm.nih.gov/pubmed/16177825 16177825]
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]
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Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase., Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5357-62. Epub 2005 Apr 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15809419 15809419]
[[Category: Clostridium botulinum d phage]]
[[Category: Clostridium botulinum d phage]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ral]]
[[Category: Ral]]
[[Category: Rho]]
[[Category: Rho]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:41:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:23:13 2008''

Revision as of 16:23, 28 July 2008

Image:2a78.png

Template:STRUCTURE 2a78

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

Template:ABSTRACT PUBMED 16177825

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

Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase., Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5357-62. Epub 2005 Apr 4. PMID:15809419

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