1pux
From Proteopedia
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'''NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers''' | '''NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers''' | ||
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[[Category: Volkman, B F.]] | [[Category: Volkman, B F.]] | ||
[[Category: Wemmer, D E.]] | [[Category: Wemmer, D E.]] | ||
| - | [[Category: | + | [[Category: Beryllofluoride]] |
| - | [[Category: | + | [[Category: Phosphorelay]] |
| - | [[Category: | + | [[Category: Response regulator]] |
| - | + | [[Category: Sporulation]] | |
| - | [[Category: | + | [[Category: Two-component system]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:30:43 2008'' |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:30, 3 May 2008
NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers
Overview
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.
About this Structure
1PUX is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system., Gardino AK, Volkman BF, Cho HS, Lee SY, Wemmer DE, Kern D, J Mol Biol. 2003 Aug 1;331(1):245-54. PMID:12875849 Page seeded by OCA on Sat May 3 05:30:43 2008
