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The three‐dimensional structure of α1‐purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics
Author(s) -
Clore G. Marius,
Nilges Michael,
Sukumaran Dinesh K.,
Brünger Axel T.,
Karplus Martin,
Gronenborn Angela M.
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04557.x
Subject(s) - vicinal , nuclear overhauser effect , dihedral angle , geometry , molecular dynamics , torsion (gastropod) , nuclear magnetic resonance , molecular geometry , physics , resonance (particle physics) , crystallography , proton , hydrogen bond , nuclear magnetic resonance spectroscopy , molecular physics , molecule , atomic physics , mathematics , biology , chemistry , quantum mechanics , zoology
The determination of the three‐dimensional solution structure of α1‐purothionin using a combination of metric matrix distance geometry and restrained molecular dynamics calculations based on n.m.r. data is presented. The experimental data comprise complete sequence‐specific proton resonance assignments, a set of 310 approximate interproton distance restraints derived from nuclear Overhauser effects, 27 Ø backbone torsion angle restraints derived from vicinal coupling constants, 4 distance restraints from hydrogen bonds and 12 distance restraints from disulphide bridges. The average atomic rms difference between the final nine converged structures and the mean structure obtained by averaging their coordinates is 1.5 ± 0.1 å for the backbone atoms and 2.0 ± 0.1 å for all atoms. The overall shape of α1‐purothionin is that of the capital letter L, similar to that of crambin, with the longer arm comprising two approximately parallel α‐helices and the shorter arm a strand and a mini anti‐parallel β sheet.