3b4b: Difference between revisions

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==Overview==

The glmS ribozyme is a catalytic riboswitch that is activated for, endonucleolytic cleavage by the coenzyme glucosamine-6-phosphate. Using, kinetic assays and X-ray crystallography, we identify an active-site, mutation of a conserved guanine that abolishes catalysis without, perturbing coenzyme binding. Our results provide evidence that coenzyme, function requires a specific nucleobase to interact with the nucleophile, of the cleavage reaction.

The glmS ribozyme is a catalytic riboswitch that is activated for endonucleolytic cleavage by the coenzyme glucosamine-6-phosphate. Using kinetic assays and X-ray crystallography, we identify an active-site mutation of a conserved guanine that abolishes catalysis without perturbing coenzyme binding. Our results provide evidence that coenzyme function requires a specific nucleobase to interact with the nucleophile of the cleavage reaction.

==About this Structure==

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[[Category: Protein complex]]

[[Category: Thermoanaerobacter tengcongensis]]

[[Category: Amare, A.R.Ferre-D.]]

[[Category: Amare, A R.Ferre-D.]]

[[Category: Klein, D.J.]]

[[Category: Klein, D J.]]

[[Category: 3AD]]

[[Category: GLP]]

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[[Category: rna]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:03:13 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The glmS ribozyme is a catalytic riboswitch that is activated for, endonucleolytic cleavage by the coenzyme glucosamine-6-phosphate. Using, kinetic assays and X-ray crystallography, we identify an active-site, mutation of a conserved guanine that abolishes catalysis without, perturbing coenzyme binding. Our results provide evidence that coenzyme, function requires a specific nucleobase to interact with the nucleophile, of the cleavage reaction.
+The glmS ribozyme is a catalytic riboswitch that is activated for endonucleolytic cleavage by the coenzyme glucosamine-6-phosphate. Using kinetic assays and X-ray crystallography, we identify an active-site mutation of a conserved guanine that abolishes catalysis without perturbing coenzyme binding. Our results provide evidence that coenzyme function requires a specific nucleobase to interact with the nucleophile of the cleavage reaction.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Thermoanaerobacter tengcongensis]]
-[[Category: Amare, A.R.Ferre-D.]]
+[[Category: Amare, A R.Ferre-D.]]
-[[Category: Klein, D.J.]]
+[[Category: Klein, D J.]]
 [[Category: 3AD]]
 [[Category: GLP]]
@@ Line 23: / Line 23: @@
 [[Category: rna]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:47:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:03:13 2008''