Exoenzyme
From Proteopedia
(Difference between revisions)
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<scene name='59/593306/Cv/7'>ADP binding site</scene> in exoenzyme C3 catalytic domain (PDB code [[2c8c]]). <ref>PMID:18369192</ref> | <scene name='59/593306/Cv/7'>ADP binding site</scene> in exoenzyme C3 catalytic domain (PDB code [[2c8c]]). <ref>PMID:18369192</ref> | ||
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| + | ==3D structures of exoenzyme== | ||
| + | [[Exoenzyme 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
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**[[1he1]] – PaExo S GAP domain + Ras-like protein + GDP <br /> | **[[1he1]] – PaExo S GAP domain + Ras-like protein + GDP <br /> | ||
**[[1he9]] – PaExo S GAP domain + Ras-like protein <br /> | **[[1he9]] – PaExo S GAP domain + Ras-like protein <br /> | ||
| + | **[[6gn0]], [[6gn8]], [[6gnj]] – PaExo S residues 235-457 (mutant) + 14-3-3 protein β/α<br /> | ||
| + | **[[6gnk]] – PaExo S residues 235-457 (mutant) + 14-3-3 protein β/α + NAD derivative<br /> | ||
**[[4zua]] – PaExo SA regulatory domain residues 2-178 <br /> | **[[4zua]] – PaExo SA regulatory domain residues 2-178 <br /> | ||
**[[3kxy]] – PaExo SC residues 1-133 + PaExo SE residues 16-81<br /> | **[[3kxy]] – PaExo SC residues 1-133 + PaExo SE residues 16-81<br /> | ||
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**[[4jmf]] – PaExo residues 28-77 + chaperone<br /> | **[[4jmf]] – PaExo residues 28-77 + chaperone<br /> | ||
| + | **[[6jnp]] – PaExo residues 23-79 + YOPE rgulator<br /> | ||
| + | **[[6gnn]] – PaExo residues 235-457 + 14-3-3 protein β/α<br /> | ||
}} | }} | ||
Revision as of 06:35, 25 June 2019
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3D structures of exoenzyme
Updated on 25-June-2019
References
- ↑ 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
