Sulphur-aromatic interactions in proteins

The geometry of sulphur-aromatic interactions in globular proteins has been analysed using crystallographic data derived from 36 proteins, solved to resolutions of 2 Å or better. About half of all sulphur atoms from cyst(e)ine and methionine residues are in contact ( ≦ 6 Å from ring centroid) with a...

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Bibliographic Details
Published in:FEBS letters 1985-10, Vol.190 (2), p.209-213
Main Authors: Reid, K.S.C., Lindley, P.F., Thornton, J.M.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
geometry
Molecular biophysics
proteins
Structure in molecular biology
sulfur
Tridimensional structure
X-ray diffraction
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Summary:The geometry of sulphur-aromatic interactions in globular proteins has been analysed using crystallographic data derived from 36 proteins, solved to resolutions of 2 Å or better. About half of all sulphur atoms from cyst(e)ine and methionine residues are in contact ( ≦ 6 Å from ring centroid) with an aromatic ring (phenylalanine, tyrosine or tryptophan). Compared to carbon and nitrogen atoms the interacting sulphur atoms express an affinity towards the edge of the aromatic rings, and avoid the region above the ring in the vicinity of the π-electrons. This preference is similar to that previously found for oxygen atoms around phenylalanine rings, and may be electrostatic in origin. Sulfw-aromatic interaction Protein Side-chain contact Cyst(e)ine Methionine Packing
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)81285-0