This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1pux

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(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...)
Next diff →

Revision as of 22:01, 20 November 2007


1pux

Drag the structure with the mouse to rotate

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 Wed Nov 21 00:08:29 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools