1pux
From Proteopedia
(New page: 200px<br /><applet load="1pux" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pux" /> '''NMR Solution Structure of BeF3-Activated Spo...) |
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| - | [[Image:1pux.gif|left|200px]]<br /><applet load="1pux" size=" | + | [[Image:1pux.gif|left|200px]]<br /><applet load="1pux" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers'''<br /> | '''NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two-component systems, which are comprised of a single histidine-aspartate | + | 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== | ==About this Structure== | ||
| - | 1PUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1PUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cho, H | + | [[Category: Cho, H S.]] |
| - | [[Category: Gardino, A | + | [[Category: Gardino, A K.]] |
[[Category: Kern, D.]] | [[Category: Kern, D.]] | ||
| - | [[Category: Lee, S | + | [[Category: Lee, S Y.]] |
| - | [[Category: Volkman, B | + | [[Category: Volkman, B F.]] |
| - | [[Category: Wemmer, D | + | [[Category: Wemmer, D E.]] |
[[Category: (beta/alpha)5 barrel]] | [[Category: (beta/alpha)5 barrel]] | ||
[[Category: beryllofluoride]] | [[Category: beryllofluoride]] | ||
| Line 26: | Line 26: | ||
[[Category: two-component systems]] | [[Category: two-component systems]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:45 2008'' |
Revision as of 12:32, 21 February 2008
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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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