1pux
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= SPO0F ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= SPO0F ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fsp|1FSP]], [[2fsp|2FSP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pux OCA], [http://www.ebi.ac.uk/pdbsum/1pux PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pux RCSB]</span> | ||
}} | }} | ||
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[[Category: two-component system]] | [[Category: two-component system]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:04:50 2008'' |
Revision as of 20:04, 30 March 2008
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| Gene: | SPO0F (Bacillus subtilis) | ||||||
| Related: | 1FSP, 2FSP
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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