Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus anthracis / enzymology
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Bacillus anthracis / genetics
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Binding Sites
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Catalysis
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Crystallography, X-Ray
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Guanine / chemistry*
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Guanine / metabolism*
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Models, Molecular
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Molecular Structure
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Mutation / genetics
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RNA, Catalytic / chemistry*
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RNA, Catalytic / genetics
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RNA, Catalytic / metabolism*
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Thermoanaerobacter / enzymology
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Thermoanaerobacter / genetics
Associated data
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PDB/3B4A
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PDB/3B4B
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PDB/3B4C