3PY9

X-ray structural studies of the entire extra-cellular region of the Ser/Thr kinase PrkC from Staphylococcus aureus

3PY9 の概要

• エントリーDOI: 10.2210/pdb3py9/pdb
• 分子名称: Protein kinase, EUROPIUM ION (3 entities in total)
• 機能のキーワード: pasta, kinase, muropeptide binding, phosphorylation, membrane, transferase
• 由来する生物種: Staphylococcus aureus subsp. aureus Mu50
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33314.47

構造登録者

Ruggiero, A.,Squeglia, F.,Marasco, D.,Marchetti, R.,Molinaro, A.,Berisio, R. (登録日: 2010-12-12, 公開日: 2011-01-19, 最終更新日: 2024-02-21)

主引用文献

Ruggiero, A.,Squeglia, F.,Marasco, D.,Marchetti, R.,Molinaro, A.,Berisio, R.
X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus.
Biochem.J., 435:33-41, 2011

PubMed Abstract: Bacterial serine/threonine kinases modulate a wide number of cellular processes. The serine/threonine kinase PrkC from the human pathogen Staphylococcus aureus was also shown to induce germination of Bacillus subtilis spores, in response to cell wall muropeptides. The presence of muropeptides in the bacterial extracellular milieu is a strong signal that the growing conditions are promising. In the present paper, we report the X-ray structure of the entire extracellular region of PrkC from S. aureus. This structure reveals that the extracellular region of PrkC, EC-PrkC, is a linear modular structure composed of three PASTA (penicillin binding-associated and serine/threonine kinase-associated) domains and an unpredicted C-terminal domain, which presents the typical features of adhesive proteins. Using several solution techniques, we also found that EC-PrkC shows no tendency to dimerize even in the presence of high concentrations of muropeptides. X-ray structural results obtained in the present study provide molecular clues into the mechanism of muropeptide-induced PrkC activation.

PubMed: 21208192
DOI: 10.1042/BJ20101643

実験手法

X-RAY DIFFRACTION (2.2 Å)