1pux | pdb_00001pux

NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers

spinqualitylabelsall models 1pux, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pux is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1fsp, 2fsp Gene: SPO0F ("Vibrio subtilis" Ehrenberg 1835) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SP0F_BACSU] Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotransferase 3D structures

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