2C8C

Structure of the ARTT motif Q212A mutant C3bot1 Exoenzyme (NAD-bound state, crystal form I)

Summary for 2C8C

• Entry DOI: 10.2210/pdb2c8c/pdb
• Related: 1G24 1GZE 1GZF 1UZI 2A78 2A9K 2BOV 2C89 2C8A 2C8B 2C8D 2C8E 2C8F 2C8G 2C8H
• Descriptor: MONO-ADP-RIBOSYLTRANSFERASE C3, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: c3 exoenzyme, artt motif, bacterial toxins, glycosyltransferase, transferase
• Biological source: CLOSTRIDIUM BOTULINUM
• Cellular location: Secreted: P15879
• Total number of polymer chains: 4
• Total formula weight: 96557.15

Authors

Stura, E.A.,Menetrey, J.,Flatau, G.,Boquet, P.,Menez, A. (deposition date: 2005-12-03, release date: 2007-02-27, Last modification date: 2023-12-13)

Primary citation

Menetrey, J.,Flatau, G.,Boquet, P.,Menez, A.,Stura, E.A.
Structural Basis for the Nad-Hydrolysis Mechanism and the Artt-Loop Plasticity of C3 Exoenzymes.
Protein Sci., 17:878-, 2008

PubMed Abstract: C3-like exoenzymes are ADP-ribosyltransferases that specifically modify some Rho GTPase proteins, leading to their sequestration in the cytoplasm, and thus inhibiting their regulatory activity on the actin cytoskeleton. This modification process goes through three sequential steps involving NAD-hydrolysis, Rho recognition, and binding, leading to Rho ADP-ribosylation. Independently, three distinct residues within the ARTT loop of the C3 exoenzymes are critical for each of these steps. Supporting the critical role of the ARTT loop, we have shown previously that it adopts a distinct conformation upon NAD binding. Here, we present seven wild-type and ARTT loop-mutant structures of C3 exoenzyme of Clostridium botulinum free and bound to its true substrate, NAD, and to its NAD-hydrolysis product, nicotinamide. Altogether, these structures expand our understanding of the conformational diversity of the C3 exoenzyme, mainly within the ARTT loop.

PubMed: 18369192
DOI: 10.1110/PS.073398508

Experimental method

X-RAY DIFFRACTION (2.7 Å)