1G9K

CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18

1G9K の概要

• エントリーDOI: 10.2210/pdb1g9k/pdb
• 関連するPDBエントリー: 1KAP 1SAT
• 分子名称: SERRALYSIN, CALCIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: beta jelly roll, hydrolase
• 由来する生物種: Pseudomonas
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49169.63

構造登録者

Aghajari, N.,Haser, R. (登録日: 2000-11-24, 公開日: 2003-02-14, 最終更新日: 2023-08-09)

主引用文献

Aghajari, N.,Van Petegem, F.,Villeret, V.,Chessa, J.P.,Gerday, C.,Haser, R.,Van Beeumen, J.
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases
Proteins, 50:636-647, 2003

PubMed Abstract: Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation and transformation of the substrates at low energy costs. Here, we report the structures of two crystal forms of the alkaline protease from an Antarctic Pseudomonas species (PAP), solved to 2.1- and 1.96-A resolution, respectively. Comparative studies of PAP structures with mesophilic counterparts show that the overall structures are similar but that the conformation of the substrate-free active site in PAP resembles that of the substrate-bound region of the mesophilic homolog, with both an active-site tyrosine and a substrate-binding loop displaying a conformation as in the substrate-bound form of the mesophilic proteases. Further, a region in the catalytic domain of PAP undergoes a conformational change with a loop movement as large as 13 A, induced by the binding of an extra calcium ion. Finally, the active site is more accessible due to deletions occurring in surrounding loop regions.

PubMed: 12577270
DOI: 10.1002/prot.10264

実験手法

X-RAY DIFFRACTION (1.96 Å)