2B6N

The 1.8 A crystal structure of a Proteinase K like enzyme from a psychrotroph Serratia species

2B6N の概要

• エントリーDOI: 10.2210/pdb2b6n/pdb
• 分子名称: proteinase K, TRIPEPTIDE, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: s binding, substrate specificity, proteinase k, subtilase, psychrotrophic, psychrophilic, hydrolase
• 由来する生物種: Serratia sp.; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28842.08

構造登録者

Helland, R.,Larsen, A.N.,Smalas, A.O.,Willassen, N.P. (登録日: 2005-10-03, 公開日: 2006-03-07, 最終更新日: 2024-11-06)

主引用文献

Helland, R.,Larsen, A.N.,Smalas, A.O.,Willassen, N.P.
The 1.8 A crystal structure of a proteinase K-like enzyme from a psychrotroph Serratia species
Febs J., 273:61-71, 2006

PubMed Abstract: Proteins from organisms living in extreme conditions are of particular interest because of their potential for being templates for redesign of enzymes both in biotechnological and other industries. The crystal structure of a proteinase K-like enzyme from a psychrotroph Serratia species has been solved to 1.8 A. The structure has been compared with the structures of proteinase K from Tritirachium album Limber and Vibrio sp. PA44 in order to reveal structural explanations for differences in biophysical properties. The Serratia peptidase shares around 40 and 64% identity with the Tritirachium and Vibrio peptidases, respectively. The fold of the three enzymes is essentially identical, with minor exceptions in surface loops. One calcium binding site is found in the Serratia peptidase, in contrast to the Tritirachium and Vibrio peptidases which have two and three, respectively. A disulfide bridge close to the S2 site in the Serratia and Vibrio peptidases, an extensive hydrogen bond network in a tight loop close to the substrate binding site in the Serratia peptidase and different amino acid sequences in the S4 sites are expected to cause different substrate specificity in the three enzymes. The more negative surface potential of the Serratia peptidase, along with a disulfide bridge close to the S2 binding site of a substrate, is also expected to contribute to the overall lower binding affinity observed for the Serratia peptidase. Clear electron density for a tripeptide, probably a proteolysis product, was found in the S' sites of the substrate binding cleft.

PubMed: 16367748
DOI: 10.1111/j.1742-4658.2005.05040.x

実験手法

X-RAY DIFFRACTION (1.8 Å)