2NZ4

Structural investigation of the GlmS ribozyme bound to its catalytic cofactor

Summary for 2NZ4

• Entry DOI: 10.2210/pdb2nz4/pdb
• Descriptor: substrate strand RNA 13-mer, GlmS ribozyme, U1 Small Nuclear Ribonucleoprotein A, ... (6 entities in total)
• Functional Keywords: structural protein/rna, structural protein-rna complex
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P09012
• Total number of polymer chains: 12
• Total formula weight: 244402.54

Authors

Cochrane, J.C. (deposition date: 2006-11-22, release date: 2007-01-16, Last modification date: 2023-12-27)

Primary citation

Cochrane, J.C.,Lipchock, S.V.,Strobel, S.A.
Structural Investigation of the GlmS Ribozyme Bound to Its Catalytic Cofactor
Chem.Biol., 14:97-105, 2007

PubMed Abstract: 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 A 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.

PubMed: 17196404
DOI: 10.1016/j.chembiol.2006.12.005

Experimental method

X-RAY DIFFRACTION (2.498 Å)