1PV0

Structure of the Sda antikinase

1PV0 の概要

• エントリーDOI: 10.2210/pdb1pv0/pdb
• NMR情報: BMRB: 5847
• 分子名称: Sda (1 entity in total)
• 機能のキーワード: sda, kina, antikinase, histidine kinase, sporulation phosphorelay, signaling protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5448.28

構造登録者

Rowland, S.L.,Burkholder, W.F.,Maciejewski, M.W.,Grossman, A.D.,King, G.F. (登録日: 2003-06-26, 公開日: 2004-04-13, 最終更新日: 2024-05-22)

主引用文献

Rowland, S.L.,Burkholder, W.F.,Cunningham, K.A.,Maciejewski, M.W.,Grossman, A.D.,King, G.F.
Structure and mechanism of Sda: an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis
Mol.Cell, 13:689-701, 2004

PubMed Abstract: 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.

PubMed: 15023339
DOI: 10.1016/S1097-2765(04)00084-X

実験手法

SOLUTION NMR