4HXE

Pyrococcus horikoshii acylaminoacyl peptidase (uncomplexed)

4HXE の概要

• エントリーDOI: 10.2210/pdb4hxe/pdb
• 関連するPDBエントリー: 4HXF 4HXG
• 分子名称: Putative uncharacterized protein PH0594, MAGNESIUM ION, HEXANE-1,6-DIOL, ... (4 entities in total)
• 機能のキーワード: self-compartmentalization, beta-propeller, alpha/beta hyrdolase fold, 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: 74118.24

構造登録者

Tichy-Racs, E.,Hornung, B.,Radi, K.,Menyhard, D.K.,Kiss-Szeman, A.,Szeltner, Z.,Domokos, K.,Szamosi, I.,Naray-Szabo, G.,Polgar, L.,Harmat, V. (登録日: 2012-11-09, 公開日: 2013-05-08, 最終更新日: 2024-02-28)

主引用文献

Menyhard, D.K.,Kiss-Szeman, A.,Tichy-Racs, E.,Hornung, B.,Radi, K.,Szeltner, Z.,Domokos, K.,Szamosi, I.,Naray-Szabo, G.,Polgar, L.,Harmat, V.
A Self-compartmentalizing Hexamer Serine Protease from Pyrococcus Horikoshii: SUBSTRATE SELECTION ACHIEVED THROUGH MULTIMERIZATION.
J.Biol.Chem., 288:17884-17894, 2013

PubMed Abstract: Oligopeptidases impose a size limitation on their substrates, the mechanism of which has long been under debate. Here we present the structure of a hexameric serine protease, an oligopeptidase from Pyrococcus horikoshii (PhAAP), revealing a complex, self-compartmentalized inner space, where substrates may access the monomer active sites passing through a double-gated "check-in" system, first passing through a pore on the hexamer surface and then turning to enter through an even smaller opening at the monomers' domain interface. This substrate screening strategy is unique within the family. We found that among oligopeptidases, a residue of the catalytic apparatus is positioned near an amylogenic β-edge, which needs to be protected to prevent aggregation, and we found that different oligopeptidases use different strategies to achieve such an end. We propose that self-assembly within the family results in characteristically different substrate selection mechanisms coupled to different multimerization states.

PubMed: 23632025
DOI: 10.1074/jbc.M113.451534

実験手法

X-RAY DIFFRACTION (1.91 Å)