1PUX

NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers

Summary for 1PUX

• Entry DOI: 10.2210/pdb1pux/pdb
• Related: 1FSP 2FSP
• NMR Information: BMRB: 5899
• Descriptor: Sporulation initiation phosphotransferase F (1 entity in total)
• Functional Keywords: sporulation, (beta/alpha)5 barrel, response regulator, phosphorelay, beryllofluoride, two-component systems, transferase
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Probable): P06628
• Total number of polymer chains: 1
• Total formula weight: 14244.66

Authors

Gardino, A.K.,Volkman, B.F.,Cho, H.S.,Lee, S.Y.,Wemmer, D.E.,Kern, D. (deposition date: 2003-06-25, release date: 2003-08-19, Last modification date: 2024-05-22)

Primary citation

Gardino, A.K.,Volkman, B.F.,Cho, H.S.,Lee, S.Y.,Wemmer, D.E.,Kern, D.
The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system.
J.Mol.Biol., 331:245-254, 2003

PubMed Abstract: Two-component systems, which are comprised of a single histidine-aspartate phosphotransfer module, are the dominant signaling pathways in bacteria and have recently been identified in several eukaryotic organisms as well. A tandem connection of two or more histidine-aspartate motifs forms complex phosphorelays. While response regulators from simple two-component systems have been characterized structurally in their inactive and active forms, we address here the question of whether a response regulator from a phosphorelay has a distinct structural basis of activation. We report the NMR solution structure of BeF(3)(-)-activated Spo0F, the first structure of a response regulator from a phosphorelay in its activated state. Conformational changes were found in regions previously identified to change in simple two-component systems. In addition, a downward shift by half a helical turn in helix 1, located on the opposite side of the common activation surface, was observed as a consequence of BeF(3)(-) activation. Conformational changes in helix 1 can be rationalized by the distinct function of phosphoryl transfer to the second histidine kinase, Spo0B, because helix 1 is known to interact directly with Spo0B and the phosphatase RapB. The identification of structural rearrangements in Spo0F supports the hypothesis of a pre-existing equilibrium between the inactive and active state prior to phosphorylation that was suggested on the basis of previous NMR dynamics studies on Spo0F. A shift of a pre-existing equilibrium is likely a general feature of response regulators.

PubMed: 12875849
DOI: 10.1016/S0022-2836(03)00733-2

Experimental method

SOLUTION NMR