1meg: Difference between revisions

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[[Category: thiol protease]]
[[Category: thiol protease]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:18:04 2007''
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Revision as of 16:38, 30 October 2007

File:1meg.gif


1meg, resolution 2.0Å

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CRYSTAL STRUCTURE OF A CARICAIN D158E MUTANT IN COMPLEX WITH E-64

OverviewOverview

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.

About this StructureAbout this Structure

1MEG is a [Single protein] structure of sequence from [Carica papaya] with E64 and EOH as [ligands]. Active as [Caricain], with EC number [3.4.22.30]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].

ReferenceReference

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

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