Crystal Structure of Diphtheria Toxin Bound to Nicotinamide Adenine Dinucleotide
作者： Charles E. Bell , David Eisenberg
DOI: 10.1021/BI9520848
关键词:
摘要: The crystal structure of diphtheria toxin (DT) in complex with nicotinamide adenine dinucleotide (NAD) has been determined by x-ray crystallography to 2.3A resolution. NAD binds a cleft on the surface catalytic (C) domain DT, interacting closely side chains Tyr54, Tyr65, His21, Thr23, and Glu 48. carboxylate group Glul48 DT lies approximately 4A from scissile, N-glycosidic bond NAD, suggesting possible role for 148 stabilizing positively charged oxocarbonium intermediate. Residues 39-46 active-site loop C-domain become disordered upon NAD-binding, potential these residues binding elongation facor-2 (EF-2). Structural alignments DT-NAD structures other ADP-ribosylating toxins suggest how may bind enzymes.
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