1meg

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==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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[[Category: Caricain]]
[[Category: Caricain]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Katerelos, N.A.]]
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[[Category: Katerelos, N A.]]
[[Category: E64]]
[[Category: E64]]
[[Category: EOH]]
[[Category: EOH]]
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[[Category: thiol protease]]
[[Category: thiol protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:53:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:25 2008''

Revision as of 11:54, 21 February 2008


1meg, resolution 2.0Å

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

Overview

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 Structure

1MEG is a Single protein structure of sequence from Carica papaya with and as ligands. Active as Caricain, with EC number 3.4.22.30 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

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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