4hxg: Difference between revisions
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==Pyrococcus horikoshii acylaminoacyl peptidase (orthorhombic crystal form)== | |||
<StructureSection load='4hxg' size='340' side='right'caption='[[4hxg]], [[Resolution|resolution]] 2.70Å' 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]] 2.7Å</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®/PubMed®, 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]] | |||
Latest revision as of 15:12, 20 September 2023
Pyrococcus horikoshii acylaminoacyl peptidase (orthorhombic crystal form)
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