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Crystal structure of a protein‐toxin α~1~‐purothionin at 2.5Å and a comparison with predicted models by Dr. Martha M. Teeter; Xing-Qi Ma; Usha Rao; Marc Whitlow is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract α~1~‐Purothionin (α~1~‐P), a wheatgerm protein and lytic toxin, has a secondary and tertiary structure similar to that of crambin as revealed by CD and NMR studies. α~1~‐P crystallizes in the tetragonal space group I422 with unit cell dimensions: __a__ = __b__ = 53.59 and __c__ = 69.79 Å. X‐ray diffraction data have been measured to 2.5 Å Bragg spacing. The crystal structure has been determined by molecular replacement methods, using an energy‐minimized α~1~‐P model structure derived from crambin (Whitlow and Teeter: __Journal of Biomolecular Structure and Dynamics__ 2:831–848, 1985, __Journal of the American Chemical Society__ 108:7163–7172, 1986). The energy‐minimized model gives a slightly cleaner rotation solution and better refinement against the x‐ray data than do the crambin or unminimized α~1~‐P structures. The final crystallographic residual with the data in the 10–2.5 Å resolution range is 0.216. The refined α~1~‐P structure has a backbone rms difference of 0.74 Å from crambin and 0.55 Å from the energy‐minimized α~1~‐P model. A low resolution NMR model of α~1~‐P calculated from metric matrix distance geometry and restrained molecular dynamics differs from cra

Who reads Crystal structure of a protein‐toxin α~1~‐purothionin at 2.5Å and a comparison with predicted models?

Author

Dr. Martha M. Teeter; Xing-Qi Ma; Usha Rao; Marc Whitlow

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

1990

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)