2GOP

The beta-propeller domain of the Trilobed protease from Pyrococcus furiosus reveals an open velcro topology

2GOP の概要

• エントリーDOI: 10.2210/pdb2gop/pdb
• 分子名称: Trilobed Protease (2 entities in total)
• 機能のキーワード: beta propeller, open velcro, hydrolase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82217.05

構造登録者

Bosch, J.,Tamura, T.,Tamura, N.,Baumeister, W.,Essen, L.-O. (登録日: 2006-04-13, 公開日: 2007-01-23, 最終更新日: 2024-02-14)

主引用文献

Bosch, J.,Tamura, T.,Tamura, N.,Baumeister, W.,Essen, L.O.
The beta-propeller domain of the trilobed protease from Pyrococcus furiosus reveals an open Velcro topology.
Acta Crystallogr.,Sect.D, 63:179-187, 2007

PubMed Abstract: In the proteolytic pathway of prokaryotic and eukaryotic organisms, proteins tagged for proteolysis are firstly shredded into smaller peptides by compartmentalized proteases such as the proteasome complex. Accordingly, a variety of downstream proteases have evolved to further hydrolyze these peptides to the level of free amino acids. In the search for such downstream proteases, a high-molecular-weight protease complex called trilobed protease (TLP) was recently discovered in the archaeon Pyroccocus furiosus. The crystal structure of the N-terminal beta-propeller domain of the trilobed protease at 2 A resolution shows that the trilobed protease utilizes this accessory domain to control substrate access to the active site. Modelling of the intact TLP monomer suggests that this protease has an additional side entrance to its active site as in the DPP-IV or tricorn protease complexes.

PubMed: 17242511
DOI: 10.1107/S0907444906045471

実験手法

X-RAY DIFFRACTION (2 Å)