The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding.


The structure of a Bacillus subtilis YphC/GDP complex shows that it contains two GTPase domains that pack against a central domain whose fold resembles that of an RNA binding KH-domain. Comparisons of this structure to that of a homologue in Thermotoga maritima reveals a dramatic rearrangement in the position of the N-terminal GTPase domain with a shift of… (More)


Figures and Tables

Sorry, we couldn't extract any figures or tables for this paper.

Slides referencing similar topics