Exoenzyme: Difference between revisions
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<StructureSection load='2c8c' size=' | <StructureSection load='2c8c' size='350' side='right' caption='Structure of exoenzyme C3 catalytic domain complex with ADP and NAD (PDB code [[2c8c]]).' scene='59/593306/Cv/1'> | ||
'''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<ref>PMID:11114250</ref> . | '''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<ref>PMID:11114250</ref> . |
Revision as of 14:56, 14 February 2016
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] .
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3D structures of exoenzyme3D structures of exoenzyme
Updated on 14-February-2016
ReferencesReferences
- ↑ 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