Structural highlights
Function
ARC3_CBDP ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
C3 exoenzyme from Clostridium botulinum (C3bot1) ADP-ribosylates and thereby inactivates Rho A, B and C GTPases in mammalian cells. The structure of a tetragonal crystal form has been determined by molecular replacement and refined to 1.89 A resolution. It is very similar to the apo structures determined previously from two different monoclinic crystal forms. An objective reassessment of available apo and nucleotide-bound C3bot1 structures indicates that, contrary to a previous report, the protein possesses a rigid core formed largely of beta-strands and that the general flexure that accompanies NAD binding is concentrated in two peripheral lobes. Tetragonal crystals disintegrate in the presence of NAD, most likely because of disruption of essential crystal contacts.
C3 exoenzyme from Clostridium botulinum: structure of a tetragonal crystal form and a reassessment of NAD-induced flexure.,Evans HR, Holloway DE, Sutton JM, Ayriss J, Shone CC, Acharya KR Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1502-5. Epub 2004, Jul 21. PMID:15272191[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Evans HR, Holloway DE, Sutton JM, Ayriss J, Shone CC, Acharya KR. C3 exoenzyme from Clostridium botulinum: structure of a tetragonal crystal form and a reassessment of NAD-induced flexure. Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1502-5. Epub 2004, Jul 21. PMID:15272191 doi:10.1107/S0907444904011680
