The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-Ray absorption spectroscopy.
A detailed study of the x-ray absorption spectrum of tetanus neurotoxin in the K-edge EXAFS region of the zinc absorber is presented that allows the complete identification of the amino acid residues coordinated to the zinc active site. A very satisfactory interpretation of the experimental data can be given if multiple scattering contributions are included in the analysis. Comparing the absorption spectrum of tetanus neurotoxin to that of two other structurally similar zinc-endopeptidases, thermolysin and astacin, in which the zinc coordination mode is known from crystallographic data, we conclude that in tetanus neurotoxin, besides a water molecule, zinc is coordinated to two histidines and a tyrosine.
Meneghini
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C
Laboratori Nazionali di Frascati INFN, 00044 Frascati, Italy.
Morante
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S
D015502:Absorptiometry, Photon / Q000379:methods; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D018698:Glutamic Acid; D006639:Histidine; D008666:Metalloendopeptidases / Q000737:chemistry; D009498:Neurotoxins / Q000737:chemistry*; D013744:Tetanus Toxin / Q000737:chemistry*; D013820:Thermolysin; D014443:Tyrosine; D015032:Zinc
D009498:Neurotoxins; D013744:Tetanus Toxin; D018698:Glutamic Acid; D014443:Tyrosine; D006639:Histidine; D008666:Metalloendopeptidases; C071288:astacin; D013820:Thermolysin; D015032:Zinc