4HXG

Pyrococcus horikoshii acylaminoacyl peptidase (orthorhombic crystal form)

Summary for 4HXG

• Entry DOI: 10.2210/pdb4hxg/pdb
• Related: 4HXE 4HXG
• Descriptor: Putative uncharacterized protein PH0594, HEXANE-1,6-DIOL, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: self-compartmentalization, beta-propeller, alpha/beta hyrdolase fold, hydrolase
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 12
• Total formula weight: 883497.21

Authors

Kiss-Szeman, A.,Menyhard, D.K.,Tichy-Racs, E.,Hornung, B.,Radi, K.,Szeltner, Z.,Domokos, K.,Szamosi, I.,Naray-Szabo, G.,Polgar, L.,Harmat, V. (deposition date: 2012-11-09, release date: 2013-05-08, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)