Crystallization (Comment) | Organism |
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crystals are composed of a trans-acting form of the Thermoanaerobacter tengcongensis ribozyme with a single 2'-deoxyribose substitution at the cleavage site, which traps the RNA in the precleavage state. These crystals yield an accurate structure of the RNA to 1.7 A resolution | Caldanaerobacter subterraneus subsp. tengcongensis |
Protein Variants | Comment | Organism |
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G40A | mutant with exchanged guanine is inactive. The 2.7 A resolution crystal structure of the mutant shows that the RNA is in a conformation nearly identical to that of the wild-type glmS ribozyme. The experimental electron density maps indicate that GlcN6P binds to the G40A mutant in the same location as in the wild-type ribozyme. Raman pH titrations of GlcN6P using crystals of the G40A mutant glmS ribozyme show that the pKa of the amine of the ribozyme-bound GlcN6P differs substantially for the wild-type and G40A mutant ribozymes | Caldanaerobacter subterraneus subsp. tengcongensis |
Organism | UniProt | Comment | Textmining |
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Caldanaerobacter subterraneus subsp. tengcongensis | - |
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Synonyms | Comment | Organism |
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glmS ribozyme | - |
Caldanaerobacter subterraneus subsp. tengcongensis |
Cofactor | Comment | Organism | Structure |
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additional information | glmS ribozyme employs a small-molecule cofactor. Binding of D-glucosamine 6-phosphate (GlcN6P) uncovers the latent self-cleavage activity of the RNA, which adopts a catalytically competent conformation that is nonetheless inactive in the absence of GlcN6P | Caldanaerobacter subterraneus subsp. tengcongensis |