7px8

<table><tr><td colspan='2'>[[7px8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa_domesticus Sus scrofa domesticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PX8 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7px8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7px8 OCA], [https://pdbe.org/7px8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7px8 RCSB], [https://www.ebi.ac.uk/pdbsum/7px8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7px8 ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/ACPH_PIG ACPH_PIG]] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser.

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== Publication Abstract from PubMed ==

The first structure of tetrameric mammalian acylaminoacyl peptidase, an enzyme that functions as an upstream regulator of the proteasome through the removal of terminal N-acetylated residues from its protein substrates, was determined by cryo-EM and further elucidated by MD simulations. Self-association results in a toroid-shaped quaternary structure, guided by an amyloidogenic beta-edge and unique inserts. With a Pro introduced into its central beta-sheet, sufficient conformational freedom is awarded to the segment containing the catalytic Ser587 that the serine protease catalytic triad alternates between active and latent states. Active site flexibility suggests that the dual function of catalysis and substrate selection are fulfilled by a novel mechanism: substrate entrance is regulated by flexible loops creating a double-gated channel system, while binding of the substrate to the active site is required for stabilization of the catalytic apparatus - as a second filter before hydrolysis. The structure not only underlines that within the family of S9 proteases homo-multimerization acts as a crucial tool for substrate selection, but it will also allow drug design targeting of the ubiquitin-proteasome system.

 

== References ==

[[Category: Harmat, V]]

[[Category: Hosogi, N]]

[[Category: Jakli, I]]

[[Category: Kiss-Szeman, A J]]

[[Category: Menyhard, D K]]

[[Category: Perczel, A]]

[[Category: Straner, P]]

[[Category: Tetramer]]