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Exoenzymes (Exo) are secreted by cells and break large macromolecules outside the cells. The breakdown components can pass through the cell wall. Exo C3 is a Clostridium butulinum toxin which binds NAD, splits it into ADP-ribose and nicotinamide and transfers the ADP-ribose to a protein substrate. Exo S and Exo T are secreted by Pseudomonas aeruginosa and has GTPase-activating activity as well as ADP-ribosyltransferase activity[1] .
NAD binding site.
ADP binding site in exoenzyme C3 catalytic domain (PDB code 2c8c). [2]
- ↑ Han S, Arvai AS, Clancy SB, Tainer JA. Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis. J Mol Biol. 2001 Jan 5;305(1):95-107. PMID:11114250 doi:10.1006/jmbi.2000.4292
- ↑ Menetrey J, Flatau G, Boquet P, Menez A, Stura EA. Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymes. Protein Sci. 2008 May;17(5):878-86. Epub 2008 Mar 27. PMID:18369192 doi:10.1110/ps.073398508
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3D structures of exoenzyme
Updated on 14-February-2016
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- Exoenzyme C3
- Exoenzyme C3 complexes
- 1gzf – CbExo catalytic domain + pyridinium derivative + ADP + NAD
- 2bov – CbExo + GDP + Ral-A GTPase
- 2a78 – CbExo catalytic domain + GDP + Ral-A GTPase
- 2a9k – CbExo catalytic domain+ GDP + Ral-A GTPase + NAD
- 2c8a – CbExo catalytic domain + nicotinamide
- 2c8c – CbExo catalytic domain (mutant) + ADP + NAD
- 2c8f, 2c8h – CbExo catalytic domain (mutant) + NAD
- Exoenzyme S
- 1r4t – PaExo GAP domain – Pseudomonas aeruginosa - NMR
- 1he1 – PaExo GAP domain + Ras-like protein + GDP
- 1he9 – PaExo GAP domain + Ras-like protein
- Exoenzyme T
- 4jmf – PaExo residues 28-77 + chaperone
References
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