1meg: Difference between revisions

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==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.

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==

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[[Category: Caricain]]

[[Category: Single protein]]

[[Category: Katerelos, N.A.]]

[[Category: Katerelos, N A.]]

[[Category: E64]]

[[Category: EOH]]

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[[Category: thiol protease]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Caricain]]
 [[Category: Single protein]]
-[[Category: Katerelos, N.A.]]
+[[Category: Katerelos, N A.]]
 [[Category: E64]]
 [[Category: EOH]]
@@ Line 21: / Line 21: @@
 [[Category: thiol protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:53:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:25 2008''