1pv0
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(New page: 200px<br /><applet load="1pv0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pv0" /> '''Structure of the Sda antikinase'''<br /> ==...)
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Revision as of 22:01, 20 November 2007
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Structure of the Sda antikinase
Overview
Histidine kinases are used extensively in prokaryotes to monitor and, respond to changes in cellular and environmental conditions. In Bacillus, subtilis, sporulation-specific gene expression is controlled by a, histidine kinase phosphorelay that culminates in phosphorylation of the, Spo0A transcription factor. Sda provides a developmental checkpoint by, inhibiting this phosphorelay in response to DNA damage and replication, defects. We show that Sda acts at the first step in the relay by, inhibiting autophosphorylation of the histidine kinase KinA. The structure, of Sda, which we determined using NMR, comprises a helical hairpin. A, cluster of conserved residues on one face of the hairpin mediates an, interaction between Sda and the KinA dimerization/phosphotransfer domain., This interaction stabilizes the KinA dimer, and the two proteins form a, stable heterotetramer. The data indicate that Sda forms a molecular, barricade that inhibits productive interaction between the catalytic and, phosphotransfer domains of KinA.
About this Structure
1PV0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis., Rowland SL, Burkholder WF, Cunningham KA, Maciejewski MW, Grossman AD, King GF, Mol Cell. 2004 Mar 12;13(5):689-701. PMID:15023339
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