5WQ0

Receiver domain of Spo0A from Paenisporosarcina sp. TG-14

5WQ0 の概要

• エントリーDOI: 10.2210/pdb5wq0/pdb
• 分子名称: Stage 0 sporulation protein, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: spo0a, paenisporosarcina sp. tg-14, signaling protein
• 由来する生物種: Paenisporosarcina sp. TG-14; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 113409.13

構造登録者

Lee, J.H.,Lee, C.W. (登録日: 2016-11-22, 公開日: 2017-03-22, 最終更新日: 2024-03-20)

主引用文献

Lee, C.W.,Park, S.H.,Lee, S.G.,Shin, S.C.,Han, S.J.,Kim, H.W.,Park, H.H.,Kim, S.,Kim, H.J.,Park, H.,Park, H.,Lee, J.H.
Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier
J. Microbiol., 55:464-474, 2017

PubMed Abstract: The two-component phosphorelay system is the most prevalent mechanism for sensing and transducing environmental signals in bacteria. Spore formation, which relies on the two-component phosphorelay system, enables the long-term survival of the glacial bacterium Paenisporosarcina sp. TG-14 in the extreme cold environment. Spo0A is a key response regulator of the phosphorelay system in the early stage of spore formation. The protein is composed of a regulatory N-terminal phospho-receiver domain and a DNA-binding C-terminal activator domain. We solved the three-dimensional structure of the unphosphorylated (inactive) form of the receiver domain of Spo0A (PaSpo0A-R) from Paenisporosarcina sp. TG-14. A structural comparison with phosphorylated (active form) Spo0A from Bacillus stearothermophilus (BsSpo0A) showed minor notable differences. A molecular dynamics study of a model of the active form and the crystal structures revealed significant differences in the α4 helix and the preceding loop region where phosphorylation occurs. Although an oligomerization study of PaSpo0A-R by analytical ultracentrifugation (AUC) has shown that the protein is in a monomeric state in solution, both crosslinking and crystal-packing analyses indicate the possibility of weak dimer formation by a previously undocumented mechanism. Collectively, these observations provide insight into the mechanism of phosphorylation-dependent activation unique to Spo0A.

PubMed: 28281198
DOI: 10.1007/s12275-017-6599-9

実験手法

X-RAY DIFFRACTION (2.604 Å)