Structure of the proteinase inhibitor eglin c with hydrolysed reactive centre at 2.0 Å resolution

The inhibition of serine proteinases by both synthetic and natural inhibitors has been widely studied. Eglin c is a small thermostable protein isolated from the leech, Hirudo medicinalis. Eglin c is a potent serine proteinase inhibitor. The three-dimensional structure of native eglin and of its comp...

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Bibliographic Details
Published in:	FEBS letters Vol. 317; no. 3; pp. 185 - 188
Main Authors:	Betzel, Christian, Dauter, Zbigniew, Genov, Nicolay, Lamzin, Victor, Navaza, Jorge, Schnebli, Hans Peter, Visan, Marcia, Wilson, Keith S.
Format:	Journal Article
Language:	English
Published:	Amsterdam Elsevier B.V 15-02-1993 Elsevier
Subjects:	Biological and medical sciences Crystal structure Crystalline structure Eglin c Fundamental and applied biological sciences. Psychology Hydrolysed reactive loop Hydrolysis Models, Molecular Molecular biophysics Protein Conformation Proteins Serine proteinase inhibitor Serine Proteinase Inhibitors - chemistry Serpins Structure in molecular biology Subtilisins X-Ray Diffraction Hydrolysed reactive loop Eglin c Serine proteinase inhibitor Crystal structure Enzyme Refinement Enzyme inhibitor Heavy atom method X ray diffraction Annelida Hirudo medicinalis Computerized processing Serine proteinase Hirudinea Invertebrata Conformation Crystalline structure
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Summary:	The inhibition of serine proteinases by both synthetic and natural inhibitors has been widely studied. Eglin c is a small thermostable protein isolated from the leech, Hirudo medicinalis. Eglin c is a potent serine proteinase inhibitor. The three-dimensional structure of native eglin and of its complexes with a number of proteinases are known. We here describe the crystal structure of hydrolysed eglin not bound to a proteinase. The body of the eglin has a conformation remarkably similar to that in the known complexes with proteinases. However, the peptide chain has been cut at the ‘scissile’ bond between residues 45 and 46, presumed to result from the presence of subtilisin DY in the crystallisation sample. The residues usually making up the inhibiting loop of eglin take up a quite different conformation in the nicked inhibitor leading to stabilising contacts between neighbouring molecules in the crystal. The structure was solved by molecular replacement techniques and refined to a final R-factor of 14.5%.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(93)81273-3