Structural highlights
Function
PAPA3_CARPA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 A 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.
Crystal structure of a caricain D158E mutant in complex with E-64.,Katerelos NA, Taylor MA, Scott M, Goodenough PW, Pickersgill RW FEBS Lett. 1996 Aug 19;392(1):35-9. PMID:8769310[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Katerelos NA, Taylor MA, Scott M, Goodenough PW, Pickersgill RW. Crystal structure of a caricain D158E mutant in complex with E-64. FEBS Lett. 1996 Aug 19;392(1):35-9. PMID:8769310
