Title : Crystal structure of a mutant elongation factor G trapped with a GTP analogue.

Pub. Date : 2005 Aug 15

PMID : 16083884






2 Functional Relationships(s)
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Protein Name
Organism
1 Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
2 Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens