3gcb: Difference between revisions

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==Overview==

The Gal6 protease is in a class of cysteine peptidases identified by their, ability to inactivate the anti-cancer drug bleomycin. The protein forms a, barrel structure with the active sites embedded in a channel as in the, proteasome. In Gal6 the C termini lie in the active site clefts. We show, that Gal6 acts as a carboxypeptidase on its C terminus to convert itself, to an aminopeptidase and peptide ligase. The substrate specificity of the, peptidase activity is determined by the position of the C terminus of Gal6, rather than the sequence of the substrate. We propose a model to explain, these diverse activities and Gal6's singular ability to inactivate, bleomycin.

The Gal6 protease is in a class of cysteine peptidases identified by their ability to inactivate the anti-cancer drug bleomycin. The protein forms a barrel structure with the active sites embedded in a channel as in the proteasome. In Gal6 the C termini lie in the active site clefts. We show that Gal6 acts as a carboxypeptidase on its C terminus to convert itself to an aminopeptidase and peptide ligase. The substrate specificity of the peptidase activity is determined by the position of the C terminus of Gal6 rather than the sequence of the substrate. We propose a model to explain these diverse activities and Gal6's singular ability to inactivate bleomycin.

==About this Structure==

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[[Category: Saccharomyces cerevisiae]]

[[Category: Single protein]]

[[Category: Johnston, S.A.]]

[[Category: Johnston, S A.]]

[[Category: Joshua-Tor, L.]]

[[Category: Zheng, W.]]

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[[Category: self-compartmentalizing protease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 10~~:51:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:28 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The Gal6 protease is in a class of cysteine peptidases identified by their, ability to inactivate the anti-cancer drug bleomycin. The protein forms a, barrel structure with the active sites embedded in a channel as in the, proteasome. In Gal6 the C termini lie in the active site clefts. We show, that Gal6 acts as a carboxypeptidase on its C terminus to convert itself, to an aminopeptidase and peptide ligase. The substrate specificity of the, peptidase activity is determined by the position of the C terminus of Gal6, rather than the sequence of the substrate. We propose a model to explain, these diverse activities and Gal6's singular ability to inactivate, bleomycin.
+The Gal6 protease is in a class of cysteine peptidases identified by their ability to inactivate the anti-cancer drug bleomycin. The protein forms a barrel structure with the active sites embedded in a channel as in the proteasome. In Gal6 the C termini lie in the active site clefts. We show that Gal6 acts as a carboxypeptidase on its C terminus to convert itself to an aminopeptidase and peptide ligase. The substrate specificity of the peptidase activity is determined by the position of the C terminus of Gal6 rather than the sequence of the substrate. We propose a model to explain these diverse activities and Gal6's singular ability to inactivate bleomycin.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Johnston, S.A.]]
+[[Category: Johnston, S A.]]
 [[Category: Joshua-Tor, L.]]
 [[Category: Zheng, W.]]
@@ Line 24: / Line 24: @@
 [[Category: self-compartmentalizing protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:51:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:28 2008''