Structural Investigation of the GlmS Ribozyme Bound to Its Catalytic Cofactor

Journal Article · Mon Jan 01 04:00:00 EST 2007 · Chemistry & Biology

DOI:https://doi.org/10.1016/j.chembiol.2006.12.005· OSTI ID:930621

Cochrane, J; Lipchock, S; Strobel, S

The GlmS riboswitch is located in the 5'-untranslated region of the gene encoding glucosamine-6-phosphate (GlcN6P) synthetase. The GlmS riboswitch is a ribozyme with activity triggered by binding of the metabolite GlcN6P. Presented here is the structure of the GlmS ribozyme (2.5 {angstrom} resolution) with GlcN6P bound in the active site. The GlmS ribozyme adopts a compact double pseudoknot tertiary structure, with two closely packed helical stacks. Recognition of GlcN6P is achieved through coordination of the phosphate moiety by two hydrated magnesium ions as well as specific nucleobase contacts to the GlcN6P sugar ring. Comparison of this activator bound and the previously published apoenzyme complex supports a model in which GlcN6P does not induce a conformational change in the RNA, as is typical of other riboswitches, but instead functions as a catalytic cofactor for the reaction. This demonstrates that RNA, like protein enzymes, can employ the chemical diversity of small molecules to promote catalytic activity.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 930621
• Report Number(s): BNL--80957-2008-JA
• Journal Information: Chemistry & Biology, Journal Name: Chemistry & Biology Journal Issue: 1 Vol. 14; ISSN 1074-5521
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CATALYSIS
CONFORMATIONAL CHANGES
CRYSTAL STRUCTURE
ENZYMES
GENES
MAGNESIUM IONS
METABOLITES
PHOSPHATES
PROTEINS
RNA
SACCHAROSE
national synchrotron light source