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Communication

Essential Role of an Active-Site Guanine in glmS Ribozyme Catalysis

Supporting Info

Daniel J. Klein,^† Michael D. Been,^‡ and Adrian R. Ferré-D'Amaré*^†

Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109, and Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710

J. Am. Chem. Soc., 2007, 129 (48), pp 14858–14859

DOI: 10.1021/ja0768441

Publication Date (Web): November 9, 2007

†

Fred Hutchinson Cancer Research Center.

‡

Duke University.

In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

, aferre@fhcrc.org

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.

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Published In Issue December 05, 2007
Received September 10, 2007

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Communication

Essential Role of an Active-Site Guanine in glmS Ribozyme Catalysis

Abstract

Tools

SciFinder Links

Accession Codes

History

Recommend & Share

Related Content

Ligand-Directed Dynamics of Adenine Riboswitch Conformers

Folding of the SAM Aptamer is Determined by the Formation of a K-turn-dependent Pseudoknot

Evidence for Preorganization of the glmS Ribozyme Ligand Binding Pocket

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