View source for 4hxg


==Pyrococcus horikoshii acylaminoacyl peptidase (orthorhombic crystal form)==
<StructureSection load='4hxg' size='340' side='right'caption='[[4hxg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hxg]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HXG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4hxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxg OCA], [https://pdbe.org/4hxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hxg RCSB], [https://www.ebi.ac.uk/pdbsum/4hxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O58323_PYRHO O58323_PYRHO] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:23632025</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hxg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acylaminoacyl peptidase 3D structures|Acylaminoacyl peptidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Domokos K]]
[[Category: Harmat V]]
[[Category: Hornung B]]
[[Category: Kiss-Szeman A]]
[[Category: Menyhard DK]]
[[Category: Naray-Szabo G]]
[[Category: Polgar L]]
[[Category: Radi K]]
[[Category: Szamosi I]]
[[Category: Szeltner Z]]
[[Category: Tichy-Racs E]]