Journal
JOURNAL OF BACTERIOLOGY
Volume 187, Issue 24, Pages 8221-8227Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.187.24.8221-8227.2005
Keywords
-
Categories
Funding
- NIGMS NIH HHS [GM54246, R01 GM054246] Funding Source: Medline
Ask authors/readers for more resources
Spo0F is a secondary messenger in the sporulation phosphorelay, and its structure has been characterized crystallographically in the apo-state, in the metal-bound state, and in an interacting state with a phosphotransferase. Additionally, the solution structure of the molecule has been characterized by nuclear magnetic resonance techniques in the unliganded state and in complex with beryllofluoride. Spo0F is a single-domain protein with a well-defined three-dimensional structure, but it is capable of adapting to specific conformations for catching and releasing the phosphoryl moiety. This commentary deals with the conformational fluctuations of the molecule as it moves from an apo-state to a metal-coordinated state, to a phosphorylated state, and then to a phosphoryl-transferring state.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available