4hxf

Acylaminoacyl peptidase in complex with Z-Gly-Gly-Phe-chloromethyl ketone

spinqualitylabelsall models 4hxf, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hxf is a 1 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.601Å Ligands: CL, HEZ, MG, Y3A Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O58323_PYRHO Publication Abstract from PubMed Oligopeptidases impose a size limitation on their substrates, the mechanism of which has long been in 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, 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 member of catalytic apparatus is positioned near an amylogenic beta-edge, which needs to be protected to prevent aggregation and found different strategies applied to such end. We propose that self-assembly within the family results in characteristically different substrate selection mechanisms coupled to different multimerization states. A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii - substrate selection achieved through multimerization.,Menyhard DK, Kiss-Szeman A, Tichy-Racs E, Hornung B, Radi K, Szeltner Z, Domokos K, Szamosi I, Naray-Szabo G, Polgar L, Harmat V J Biol Chem. 2013 Apr 30. PMID:23632025 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acylaminoacyl peptidase 3D structures

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