Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin Carlsberg.
The crystal structure of the molecular complex of eglin, a serine proteinase inhibitor from leeches, with subtilisin Carlsberg has been determined at 2.0 A resolution by the molecular replacement method. The complex has been refined by restrained-parameter least-squares. The present crystallographic R factor (Formula: see text) 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 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.
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D055598:Chemical Phenomena; D002621:Chemistry; D003460:Crystallization; D007865:Leeches / Q000201:enzymology; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D015843:Serpins; D013381:Subtilisins / Q000378:metabolism*; D014961:X-Ray Diffraction
D011506:Proteins; D015843:Serpins; C028656:eglin proteinase inhibitors; D013381:Subtilisins