2HRO

Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus

2HRO の概要

• エントリーDOI: 10.2210/pdb2hro/pdb
• 分子名称: Phosphoenolpyruvate-protein phosphotransferase, SULFATE ION (3 entities in total)
• 機能のキーワード: pts, protein phosphorylation, sugar transport, histidine phosphorylation, transferase
• 由来する生物種: Staphylococcus carnosus
• 細胞内の位置: Cytoplasm: P23533
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 63457.63

構造登録者

Marquez, J.A.,Reinelt, S.,Koch, B.,Engelman, R.,Hengstenberg, W.,Scheffzek, K. (登録日: 2006-07-20, 公開日: 2006-09-19, 最終更新日: 2024-02-14)

主引用文献

Reinelt, S.,Koch, B.,Engelmann, R.,Hengstenberg, W.,Scheffzek, K.
Structure of the full-length enzyme I of the phosphoenolpyruvate-dependent sugar phosphotransferase system
J.Biol.Chem., 281:32508-32515, 2006

PubMed Abstract: Enzyme I (EI) is the phosphoenolpyruvate (PEP)-protein phosphotransferase at the entry point of the PEP-dependent sugar phosphotransferase system, which catalyzes carbohydrate uptake into bacterial cells. In the first step of this pathway EI phosphorylates the heat-stable phospho carrier protein at His-15 using PEP as a phosphoryl donor in a reaction that requires EI dimerization and autophosphorylation at His-190. The structure of the full-length protein from Staphylococcus carnosus at 2.5A reveals an extensive interaction surface between two molecules in adjacent asymmetric units. Structural comparison with related domains indicates that this surface represents the biochemically relevant contact area of dimeric EI. Each monomer has an extended configuration with the phosphohistidine and heat-stable phospho carrier protein-binding domains clearly separated from the C-terminal dimerization and PEP-binding region. The large distance of more than 35A between the active site His-190 and the PEP binding site suggests that large conformational changes must occur during the process of autophosphorylation, as has been proposed for the structurally related enzyme pyruvate phosphate dikinase. Our structure for the first time offers a framework to analyze a large amount of research in the context of the full-length model.

PubMed: 16867985
DOI: 10.1074/jbc.M513721200

実験手法

X-RAY DIFFRACTION (2.5 Å)