1QS2

CRYSTAL STRUCTURE OF VIP2 WITH NAD

Summary for 1QS2

• Entry DOI: 10.2210/pdb1qs2/pdb
• Descriptor: ADP-RIBOSYLTRANSFERASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: alpha-beta protein, protein-nad complex, binary toxin, toxin
• Biological source: Bacillus cereus
• Total number of polymer chains: 1
• Total formula weight: 46219.92

Authors

Han, S.,Craig, J.A.,Putnam, C.D.,Carozzi, N.B.,Tainer, J.A. (deposition date: 1999-06-25, release date: 1999-12-29, Last modification date: 2024-02-14)

Primary citation

Han, S.,Craig, J.A.,Putnam, C.D.,Carozzi, N.B.,Tainer, J.A.
Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex.
Nat.Struct.Biol., 6:932-936, 1999

PubMed Abstract: A member of the Bacillus-produced vegetative insecticidal proteins (VIPs) possesses high specificity against the major insect pest, corn rootworms, and belongs to a class of binary toxins and regulators of biological pathways distinct from classical A-B toxins. The 1.5 A resolution crystal structure of the enzymatic ADP-ribosyltransferase component, VIP2, from Bacillus cereus reveals structurally homologous N- and C-terminal alpha/beta domains likely representing the entire class of binary toxins and implying evolutionary relationships between families of ADP-ribosylating toxins. The crystal structure of the kinetically trapped VIP2-NAD complex identifies the NAD binding cleft within the C-terminal enzymatic domain and provides a structural basis for understanding the targeting and catalysis of the medically and environmentally important binary toxins. These structures furthermore provide specific experimental results to help resolve paradoxes regarding the specific mechanism of ADP-ribosylation of actin by implicating ground state destabilization and nicotinamide product sequestration as the major driving forces for catalysis.

PubMed: 10504727
DOI: 10.1038/13300

Experimental method

X-RAY DIFFRACTION (2.7 Å)