The Complex Between Mesentericopeptidase and Eglin-C

Abstract

This study forms part of our program of investigation of the structures of different naturally occurring subtilisins. This complements the extensive work proceeding in many laboratories on the mutagenesis of the commercially available subtilisins BPN’ and Carlsberg. Our interest is in how nature has adapted the subtilisin fold to different environments and needs in the expectation that this will eventually shed light on how we can adapt the structure to our needs. The present paper describes the structure of mesentericopeptidase (henceforth SBMEP) in its 1:1 complex with the leech inhibitor eglin-C at 2.0 Å resolution. The structure of the complex has been previously published in full¹ and we here briefly summarize the major points of the analysis.