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Crystal structure of a caricain D158E mutant in complex with E‐64
Author(s) -
Katerelos Nikolaos A.,
Taylor Mark A.J.,
Scott Mandy,
Goodenough Peter W.,
Pickersgill Richard W.
Publication year - 1996
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(96)00697-7
Subject(s) - mutant , crystal structure , chemistry , glutamate receptor , hydrogen bond , protease , stereochemistry , crystallography , biochemistry , enzyme , molecule , receptor , organic chemistry , gene
The structure of the D158E mutant of caricain (previously known as papaya protease omega) in complex with E‐64 has been determined at 2.0 Å resolution (overall R factor 19.3%). The structure reveals that the substituted glutamate makes the same pattern of hydrogen bonds as the aspartate in native caricain. This was not anticipated since in the native structure there is insufficient room to accommodate the glutamate side chain. The glutamate is accommodated in the mutant by a local expansion of the structure demonstrating that small structural changes are responsible for the change in activity.