3BPP

1510-N membrane protease K138A mutant specific for a stomatin homolog from Pyrococcus horikoshii

3BPP の概要

• エントリーDOI: 10.2210/pdb3bpp/pdb
• 関連するPDBエントリー: 2DEO
• 分子名称: 1510-N membrane protease (2 entities in total)
• 機能のキーワード: membrane protease, specific for a stomatin homolog, archaea, pyrococcus, thermostable, catalytic dyad, hydrolase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25368.03

構造登録者

Yokoyama, H.,Hamamatsu, S.,Fujii, S.,Matsui, I. (登録日: 2007-12-19, 公開日: 2008-04-29, 最終更新日: 2023-11-01)

主引用文献

Yokoyama, H.,Hamamatsu, S.,Fujii, S.,Matsui, I.
Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin
J.SYNCHROTRON RADIAT., 15:254-257, 2008

PubMed Abstract: Membrane-bound proteases are involved in various regulatory functions. A previous report indicates that the N-terminal region of PH1510 (1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138), and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511. According to the crystal structure of the wild-type 1510-N in dimeric form, the active site around Ser97 is in a hydrophobic environment suitable for the hydrophobic substrates. This article reports the crystal structure of the K138A mutant of 1510-N at 2.3 A resolution. The determined structure contains one molecule per asymmetric unit, but 1510-N is active in dimeric form. Two possible sets of dimer were found from the symmetry-related molecules. One dimer is almost the same as the wild-type 1510-N. Another dimer is probably in an inactive form. The L2 loop, which is disordered in the wild-type structure, is significantly kinked at around A-138 in the K138A mutant. Thus Lys138 probably has an important role on the conformation of L2.

PubMed: 18421152
DOI: 10.1107/S0909049507068471

実験手法

X-RAY DIFFRACTION (2.3 Å)