4EQM

Structural analysis of Staphylococcus aureus serine/threonine kinase PknB

4EQM の概要

• エントリーDOI: 10.2210/pdb4eqm/pdb
• 分子名称: Protein kinase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, BENZAMIDINE (3 entities in total)
• 機能のキーワード: kinase, serine/threonine protein kinase, transferase
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 202312.87

構造登録者

Rakette, S.,Stehle, T. (登録日: 2012-04-19, 公開日: 2012-06-27, 最終更新日: 2024-02-28)

主引用文献

Rakette, S.,Donat, S.,Ohlsen, K.,Stehle, T.
Structural Analysis of Staphylococcus aureus Serine/Threonine Kinase PknB.
Plos One, 7:e39136-e39136, 2012

PubMed Abstract: Effective treatment of infections caused by the bacterium Staphylococcus aureus remains a worldwide challenge, in part due to the constant emergence of new strains that are resistant to antibiotics. The serine/threonine kinase PknB is of particular relevance to the life cycle of S. aureus as it is involved in the regulation of purine biosynthesis, autolysis, and other central metabolic processes of the bacterium. We have determined the crystal structure of the kinase domain of PknB in complex with a non-hydrolyzable analog of the substrate ATP at 3.0 Å resolution. Although the purified PknB kinase is active in solution, it crystallized in an inactive, autoinhibited state. Comparison with other bacterial kinases provides insights into the determinants of catalysis, interactions of PknB with ligands, and the pathway of activation.

PubMed: 22701750
DOI: 10.1371/journal.pone.0039136

実験手法

X-RAY DIFFRACTION (3 Å)