Exoenzyme: Difference between revisions

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*Exoenzyme S
*Exoenzyme S


**[[1r4t]] – PaExo GAP domain – ''Pseudomonas aeruginosa'' - NMR<br />
**[[1r4t]] – PaExo S GAP domain – ''Pseudomonas aeruginosa'' - NMR<br />
**[[1he1]] – PaExo GAP domain + Ras-like protein + GDP <br />
**[[1he1]] – PaExo S GAP domain + Ras-like protein + GDP <br />
**[[1he9]] – PaExo GAP domain + Ras-like protein <br />
**[[1he9]] – PaExo S GAP domain + Ras-like protein <br />
**[[4zua]] – PaExo SA regulatory domain residues 2-178 <br />
**[[3kxy]] – PaExo SC residues 1-133 + PaExo SE residues 16-81<br />


*Exoenzyme T
*Exoenzyme T

Revision as of 10:53, 22 May 2018


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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in exoenzyme C3 catalytic domain (PDB code 2c8c). [2]


Structure of exoenzyme C3 catalytic domain complex with ADP and NAD (PDB code 2c8c).

Drag the structure with the mouse to rotate

3D structures of exoenzyme3D structures of exoenzyme

Updated on 22-May-2018

ReferencesReferences

  1. 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
  2. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky