3E2D

The 1.4 A crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase

3E2D の概要

• エントリーDOI: 10.2210/pdb3e2d/pdb
• 分子名称: Alkaline phosphatase, ZINC ION, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: cold-adaptation, metalloenzyme, dimer, psychrophilic bacteria, hydrolase
• 由来する生物種: Vibrio sp. G15-21
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112404.72

構造登録者

Helland, R.,Larsen, R.L.,Asgeirsson, B. (登録日: 2008-08-05, 公開日: 2009-06-16, 最終更新日: 2024-03-20)

主引用文献

Helland, R.,Larsen, R.L.,Asgeirsson, B.
The 1.4 A crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase.
Biochim.Biophys.Acta, 1794:297-308, 2009

PubMed Abstract: Alkaline phosphatase (AP) from the cold-adapted Vibrio strain G15-21 is among the AP variants with the highest known k(cat) value. Here the structure of the enzyme at 1.4 A resolution is reported and compared to APs from E. coli, human placenta, shrimp and the Antarctic bacterium strain TAB5. The Vibrio AP is a dimer although its monomers are without the long N-terminal helix that embraces the other subunit in many other APs. The long insertion loop, previously noted as a special feature of the Vibrio AP, serves a similar function. The surface does not have the high negative charge density as observed in shrimp AP, but a positively charged patch is observed around the active site that may be favourable for substrate binding. The dimer interface has a similar number of non-covalent interactions as other APs and the "crown"-domain is the largest observed in known APs. Part of it slopes over the catalytic site suggesting that the substrates may be small molecules. The catalytic serines are refined with multiple conformations in both monomers. One of the ligands to the catalytic zinc ion in binding site M1 is directly connected to the crown-domain and is closest to the dimer interface. Subtle movements in metal ligands may help in the release of the product and/or facilitate prior dephosphorylation of the covalent intermediate. Intersubunit interactions may be a major factor for promoting active site geometries that lead to the high catalytic activity of Vibrio AP at low temperatures.

PubMed: 18977465
DOI: 10.1016/j.bbapap.2008.09.020

実験手法

X-RAY DIFFRACTION (1.4 Å)