DOI | Trouver le DOI : https://doi.org/10.1016/S0969-2126(02)00852-3 |
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Auteur | Rechercher : Michel, Gurvan1; Rechercher : Sauvé, Véronique1; Rechercher : Larocque, Robert1; Rechercher : Li, Yunge1; Rechercher : Matte, Allan1; Rechercher : Cygler, Miroslaw1 |
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Affiliation du nom | - Conseil national de recherches du Canada. Institut de recherche en biotechnologie du CNRC
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Format | Texte, Article |
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Sujet | pharmaceutical; knot; methyltranferase; S-adenosyl-L-methionine; SpoU family; 23S rRNA; ribosome maturation |
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Résumé | In Escherichia coli, RlmB catalyzes the methylation of guanosine 2251, a modification conserved in the peptidyltransferase domain of 23S rRNA. The crystal structure of this 2′O-methyltransferase has been determined at 2.5 Å resolution. RlmB consists of an N-terminal domain connected by a flexible extended linker to a catalytic C-terminal domain and forms a dimer in solution. The C-terminal domain displays a divergent methyltransferase fold with a unique knotted region, and lacks the classic AdoMet binding site features. The N-terminal domain is similar to ribosomal proteins L7 and L30, suggesting a role in 23S rRNA recognition. The conserved residues in this novel family of 2′O-methyltransferases cluster in the knotted region, suggesting the location of the catalytic and AdoMet binding sites. |
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Date de publication | 2002-10 |
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Dans | |
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Langue | anglais |
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Numéro du CNRC | 44870 |
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Numéro NPARC | 3540078 |
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Exporter la notice | Exporter en format RIS |
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Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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Identificateur de l’enregistrement | f68bfc5e-d133-4883-9eb8-70c524cf6760 |
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Enregistrement créé | 2009-03-01 |
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Enregistrement modifié | 2020-03-30 |
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