1KKL

L.casei HprK/P in complex with B.subtilis HPr

1KKL の概要

• エントリーDOI: 10.2210/pdb1kkl/pdb
• 関連するPDBエントリー: 1KKM
• 分子名称: HprK protein, PHOSPHOCARRIER PROTEIN HPR, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: phosphorylation, protein kinase, bacteria, protein/protein interaction, transferase, hydrolase-transport protein complex, hydrolase/transport protein
• 由来する生物種: Lactobacillus casei; 詳細
• 細胞内の位置: Cytoplasm: P08877
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 100271.21

構造登録者

Fieulaine, S.,Morera, S.,Poncet, S.,Galinier, A.,Janin, J.,Deutscher, J.,Nessler, S. (登録日: 2001-12-10, 公開日: 2002-08-28, 最終更新日: 2023-08-16)

主引用文献

Fieulaine, S.,Morera, S.,Poncet, S.,Mijakovic, I.,Galinier, A.,Janin, J.,Deutscher, J.,Nessler, S.
X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr.
Proc.Natl.Acad.Sci.USA, 99:13437-13441, 2002

PubMed Abstract: HPr kinase/phosphorylase (HprK/P) controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by Gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of Ser-46 of HPr and its dephosphorylation by phosphorolysis. The latter reaction uses inorganic phosphate as substrate and produces pyrophosphate. We present here two crystal structures of a complex of the catalytic domain of Lactobacillus casei HprK/P with Bacillus subtilis HPr, both at 2.8-A resolution. One of the structures was obtained in the presence of excess pyrophosphate, reversing the phosphorolysis reaction and contains serine-phosphorylated HPr. The complex has six HPr molecules bound to the hexameric kinase. Two adjacent enzyme subunits are in contact with each HPr molecule, one through its active site and the other through its C-terminal helix. In the complex with serine-phosphorylated HPr, a phosphate ion is in a position to perform a nucleophilic attack on the phosphoserine. Although the mechanism of the phosphorylation reaction resembles that of eukaryotic protein kinases, the dephosphorylation by inorganic phosphate is unique to the HprK/P family of kinases. This study provides the structure of a protein kinase in complex with its protein substrate, giving insights into the chemistry of the phospho-transfer reactions in both directions.

PubMed: 12359875
DOI: 10.1073/pnas.192368699

実験手法

X-RAY DIFFRACTION (2.8 Å)