Identification and characterization of a hitherto unknown nucleotide-binding domain and an intricate interdomain regulation in HflX-a ribosome binding GTPase

A role for HflX in 50S-biogenesis was suggested based on its similarity to other GTPases involved in this process. It possesses a G-domain, flanked by uncharacterized N- and C-terminal domains. Intriguingly, Escherichia coli HflX was shown to hydrolyze both GTP and adenosine triphosphate (ATP), and...

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Detalles Bibliográficos
Autores principales: Jain, Nikhil, Vithani, Neha, Rafay, Abu, Prakash, Balaji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2013
Materias:
Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3814362/
https://www.ncbi.nlm.nih.gov/pubmed/23956218
http://dx.doi.org/10.1093/nar/gkt705

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3814362/
https://www.ncbi.nlm.nih.gov/pubmed/23956218
http://dx.doi.org/10.1093/nar/gkt705

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