2X98

H.SALINARUM ALKALINE PHOSPHATASE

「2W0Y」から置き換えられました

2X98 の概要

• エントリーDOI: 10.2210/pdb2x98/pdb
• 分子名称: ALKALINE PHOSPHATASE, PHOSPHATE ION, ZINC ION, ... (7 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: HALOBACTERIUM SALINARUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91507.66

構造登録者

Wende, A.,Johansson, P.,Grininger, M.,Oesterhelt, D. (登録日: 2010-03-14, 公開日: 2010-05-19, 最終更新日: 2024-05-08)

主引用文献

Wende, A.,Johansson, P.,Vollrath, R.,Dyall-Smith, M.,Oesterhelt, D.,Grininger, M.
Structural and Biochemical Characterization of a Halophilic Archaeal Alkaline Phosphatase.
J.Mol.Biol., 400:52-, 2010

PubMed Abstract: Phosphate is an essential component of all cells that must be taken up from the environment. Prokaryotes commonly secrete alkaline phosphatases (APs) to recruit phosphate from organic compounds by hydrolysis. In this study, the AP from Halobacterium salinarum, an archaeon that lives in a saturated salt environment, has been functionally and structurally characterized. The core fold and the active-site architecture of the H. salinarum enzyme are similar to other AP structures. These generally form dimers composed of dominant beta-sheet structures sandwiched by alpha-helices and have well-accessible active sites. The surface of the enzyme is predicted to be highly negatively charged, like other proteins of extreme halophiles. In addition to the conserved core, most APs contain a crown domain that strongly varies within species. In the H. salinarum AP, the crown domain is made of an acyl-carrier-protein-like fold. Different from other APs, it is not involved in dimer formation. We compare the archaeal AP with its bacterial and eukaryotic counterparts, and we focus on the role of crown domains in enhancing protein stability, regulating enzyme function, and guiding phosphoesters into the active-site funnel.

PubMed: 20438737
DOI: 10.1016/J.JMB.2010.04.057

実験手法

X-RAY DIFFRACTION (1.7 Å)