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Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin Carlsberg
Author(s) -
McPhalen C.A.,
Schnebli H.P.,
James M.N.G.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80873-5
Subject(s) - subtilisin , serine , molecular replacement , stereochemistry , crystal structure , chemistry , serine protease , biochemistry , crystallography , enzyme , protease
The crystal structure of the molecular complex of eglin, a serine proteinase inhibitor from leeches, with subtilisin Carlsberg has been determined at 2.0 Å resolution by the molecular replacement method. The complex has been refined by restrained‐parameter least‐squares. The present crystallographic R factor (= Σ¦¦ F o ¦‐¦ F c ¦/σ¦ F o ¦) is 0.183. Eglin is a member of the potato inhibitor 1 family, a group of serine proteinase inhibitors lacking disulfide bonds. Eglin shows strong structural homology to CI‐2, a related inhibitor from barley seeds. The structure of subtilisin Carlsberg in this complex is very similar to the known structure of subtilisin novo , despite changes of 84 out of 274 amino acids.