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| | {{STRUCTURE_1gze| PDB=1gze | SCENE= }} | | {{STRUCTURE_1gze| PDB=1gze | SCENE= }} |
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| - | '''STRUCTURE OF THE CLOSTRIDIUM BOTULINUM C3 EXOENZYME (L177C MUTANT)'''
| + | ===STRUCTURE OF THE CLOSTRIDIUM BOTULINUM C3 EXOENZYME (L177C MUTANT)=== |
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| - | ==Overview==
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| - | We have solved the crystal structures of Clostridium botulinum C3 exoenzyme free and complexed to NAD in the same crystal form, at 2.7 and 1.95 A, respectively. The asymmetric unit contains four molecules, which, in the free form, share the same conformation. Upon NAD binding, C3 underwent various conformational changes, whose amplitudes were differentially limited in the four molecules of the crystal unit. A major rearrangement concerns the loop that contains the functionally important ARTT motif (ADP-ribosyltransferase toxin turn-turn). The ARTT loop undergoes an ample swinging motion to adopt a conformation that covers the nicotinamide moiety of NAD. In particular, Gln-212, which belongs to the ARTT motif, flips over from a solvent-exposed environment to a buried conformation in the NAD binding pocket. Mutational experiments showed that Gln-212 is neither involved in NAD binding nor in the NAD-glycohydrolase activity of C3, whereas it plays a critical role in the ADP-ribosyl transfer to the substrate Rho. We observed additional NAD-induced movements, including a crab-claw motion of a subdomain that closes the NAD binding pocket. The data emphasized a remarkable NAD-induced plasticity of the C3 binding pocket and suggest that the NAD-induced ARTT loop conformation may be favored by the C3-NAD complex to bind to the substrate Rho. Our structural observations, together with a number of mutational experiments suggest that the mechanisms of Rho ADP-ribosylation by C3-NAD may be more complex than initially anticipated.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12029083}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12029083 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12029083}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: C3 exoenzyme]] | | [[Category: C3 exoenzyme]] |
| | [[Category: Nad]] | | [[Category: Nad]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:12:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:21:51 2008'' |
Revision as of 03:21, 1 July 2008
Template:STRUCTURE 1gze
STRUCTURE OF THE CLOSTRIDIUM BOTULINUM C3 EXOENZYME (L177C MUTANT)
Template:ABSTRACT PUBMED 12029083
About this Structure
1GZE is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.
Reference
NAD binding induces conformational changes in Rho ADP-ribosylating clostridium botulinum C3 exoenzyme., Menetrey J, Flatau G, Stura EA, Charbonnier JB, Gas F, Teulon JM, Le Du MH, Boquet P, Menez A, J Biol Chem. 2002 Aug 23;277(34):30950-7. Epub 2002 May 23. PMID:12029083
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