1K32

Crystal structure of the tricorn protease

1K32 の概要

• エントリーDOI: 10.2210/pdb1k32/pdb
• 分子名称: tricorn protease (2 entities in total)
• 機能のキーワード: protein degradation, substrate gating, serine protease, beta propeller, proteasome, hydrolase
• 由来する生物種: Thermoplasma acidophilum
• 細胞内の位置: Cytoplasm: P96086
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 712080.33

構造登録者

Brandstetter, H.,Kim, J.-S.,Groll, M.,Huber, R. (登録日: 2001-10-01, 公開日: 2001-12-05, 最終更新日: 2024-02-07)

主引用文献

Brandstetter, H.,Kim, J.S.,Groll, M.,Huber, R.
Crystal structure of the tricorn protease reveals a protein disassembly line.
Nature, 414:466-470, 2001

PubMed Abstract: The degradation of cytosolic proteins is carried out predominantly by the proteasome, which generates peptides of 7-9 amino acids long. These products need further processing. Recently, a proteolytic system was identified in the model organism Thermoplasma acidophilum that performs this processing. The hexameric core protein of this modular system, referred to as tricorn protease, is a 720K protease that is able to assemble further into a giant icosahedral capsid, as determined by electron microscopy. Here, we present the crystal structure of the tricorn protease at 2.0 A resolution. The structure reveals a complex mosaic protein whereby five domains combine to form one of six subunits, which further assemble to form the 3-2-symmetric core protein. The structure shows how the individual domains coordinate the specific steps of substrate processing, including channelling of the substrate to, and the product from, the catalytic site. Moreover, the structure shows how accessory protein components might contribute to an even more complex protein machinery that efficiently collects the tricorn-released products.

PubMed: 11719810
DOI: 10.1038/35106609

実験手法

X-RAY DIFFRACTION (2 Å)