1pux: Difference between revisions

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[[Image:1pux.gif|left|200px]]
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[[Image:1pux.png|left|200px]]


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{{STRUCTURE_1pux|  PDB=1pux  |  SCENE=  }}  
{{STRUCTURE_1pux|  PDB=1pux  |  SCENE=  }}  


'''NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers'''
===NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12875849}}


==About this Structure==
==About this Structure==
1PUX is a [[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].  
1PUX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUX OCA].  


==Reference==
==Reference==
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[[Category: Sporulation]]
[[Category: Sporulation]]
[[Category: Two-component system]]
[[Category: Two-component system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:28:58 2008''

Revision as of 00:28, 28 July 2008

File:1pux.png

Template:STRUCTURE 1pux

NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers

Template:ABSTRACT PUBMED 12875849

About this Structure

1PUX is a Single protein structure of sequence from Bacillus subtilis. Full experimental 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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