1QMP

Phosphorylated aspartate in the crystal structure of the sporulation response regulator, Spo0A

1QMP の概要

• エントリーDOI: 10.2210/pdb1qmp/pdb
• 分子名称: Stage 0 sporulation protein A, CALCIUM ION (3 entities in total)
• 機能のキーワード: replication, response regulator
• 由来する生物種: Geobacillus stearothermophilus (Bacillus stearothermophilus)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 59460.52

構造登録者

Lewis, R.J.,Brannigan, J.A.,Muchova, K.,Barak, I.,Wilkinson, A.J. (登録日: 1999-10-04, 公開日: 1999-11-14, 最終更新日: 2024-05-01)

主引用文献

Lewis, R.J.,Brannigan, J.A.,Muchova, K.,Barak, I.,Wilkinson, A.J.
Phosphorylated aspartate in the structure of a response regulator protein.
J. Mol. Biol., 294:9-15, 1999

PubMed Abstract: Phosphorylation of aspartic acid residues is the hallmark of two- component signal transduction systems that orchestrate the adaptive responses of micro-organisms to changes in their surroundings. Two-component systems consist of a sensor kinase that interprets environmental signals and a response regulator that activates the appropriate physiological response. Although structures of response regulators are known, little is understood about their activated phosphorylated forms, due to the intrinsic instability of the acid phosphate linkage. Here, we report the phosphorylated structure of the receiver/phosphoacceptor domain of Spo0A, the master regulator of sporulation, from Bacillus stearothermophilus. The phosphoryl group is covalently bonded to the invariant aspartate 55, and co-ordinated to a nearby divalent metal cation, with both species fulfilling their electrostatic potential through interactions with solvent water molecules, the protein main chain, and with side-chains of amino acid residues strongly conserved across the response regulator family. This is the first direct visualisation of a phosphoryl group covalently linked to an aspartic acid residue in any protein, with implications for signalling within the response regulator family.

PubMed: 10556024
DOI: 10.1006/jmbi.1999.3261

実験手法

X-RAY DIFFRACTION (2 Å)