Cargando…
Distinct GDP/GTP bound states of the tandem G-domains of EngA regulate ribosome binding
EngA, a unique GTPase containing a KH-domain preceded by two consecutive G-domains, displays distinct nucleotide binding and hydrolysis activities. So far, Escherichia coli EngA is reported to bind the 50S ribosomal subunit in the guanosine-5′-trihosphate (GTP) bound state. Here, for the first time,...
Autores principales: | Tomar, Sushil Kumar, Dhimole, Neha, Chatterjee, Moon, Prakash, Balaji |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2673443/ https://www.ncbi.nlm.nih.gov/pubmed/19246542 http://dx.doi.org/10.1093/nar/gkp107 |
Ejemplares similares
-
Structural insights into the function of a unique tandem GTPase EngA in bacterial ribosome assembly
por: Zhang, Xiaoxiao, et al.
Publicado: (2014) -
Extended C-terminus and length of the linker connecting the G-domains are species-specific variations in the EngA family of GTPases
por: Tomar, Sushil Kumar, et al.
Publicado: (2012) -
The ribosome assembly GTPase EngA is involved in redox signaling in cyanobacteria
por: Llop, Antonio, et al.
Publicado: (2023) -
Regulatory Connections Between the Cyanobacterial Factor PipX and the Ribosome Assembly GTPase EngA
por: Jerez, Carmen, et al.
Publicado: (2021) -
Characterizing a novel CMK-EngA fusion protein from Bifidobacterium: Implications for inter-domain regulation
por: Suresh, Ammu, et al.
Publicado: (2022)