1QS2

CRYSTAL STRUCTURE OF VIP2 WITH NAD

1QS2 の概要

• エントリーDOI: 10.2210/pdb1qs2/pdb
• 分子名称: ADP-RIBOSYLTRANSFERASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: alpha-beta protein, protein-nad complex, binary toxin, toxin
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46219.92

構造登録者

Han, S.,Craig, J.A.,Putnam, C.D.,Carozzi, N.B.,Tainer, J.A. (登録日: 1999-06-25, 公開日: 1999-12-29, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.7 Å)