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4hxe

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Pyrococcus horikoshii acylaminoacyl peptidase (uncomplexed)

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Retrieved from "http://52.214.119.220/wiki/index.php/4hxe"

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 ==Pyrococcus horikoshii acylaminoacyl peptidase (uncomplexed)==
-<StructureSection load='4hxe' size='340' side='right' caption='[[4hxe]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
+<StructureSection load='4hxe' size='340' side='right'caption='[[4hxe]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4hxe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrho Pyrho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HXE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4hxe]] is a 1 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=4HXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HXE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hxf|4hxf]], [[4hxg|4hxg]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PH0594 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 PYRHO])</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=4hxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxe OCA], [https://pdbe.org/4hxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hxe RCSB], [https://www.ebi.ac.uk/pdbsum/4hxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxe ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxe OCA], [http://pdbe.org/4hxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hxe RCSB], [http://www.ebi.ac.uk/pdbsum/4hxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxe ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/O58323_PYRHO O58323_PYRHO]
-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>
+==See Also==
+*[[Acylaminoacyl peptidase 3D structures|Acylaminoacyl peptidase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4hxe" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Acylaminoacyl-peptidase]]
+[[Category: Large Structures]]
-[[Category: Pyrho]]
+[[Category: Pyrococcus horikoshii OT3]]
-[[Category: Domokos, K]]
+[[Category: Domokos K]]
-[[Category: Harmat, V]]
+[[Category: Harmat V]]
-[[Category: Hornung, B]]
+[[Category: Hornung B]]
-[[Category: Kiss-Szeman, A]]
+[[Category: Kiss-Szeman A]]
-[[Category: Menyhard, D K]]
+[[Category: Menyhard DK]]
-[[Category: Naray-Szabo, G]]
+[[Category: Naray-Szabo G]]
-[[Category: Polgar, L]]
+[[Category: Polgar L]]
-[[Category: Radi, K]]
+[[Category: Radi K]]
-[[Category: Szamosi, I]]
+[[Category: Szamosi I]]
-[[Category: Szeltner, Z]]
+[[Category: Szeltner Z]]
-[[Category: Tichy-Racs, E]]
+[[Category: Tichy-Racs E]]
-[[Category: Alpha/beta hyrdolase fold]]
-[[Category: Beta-propeller]]
-[[Category: Hydrolase]]
-[[Category: Self-compartmentalization]]

4hxe

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Pyrococcus horikoshii acylaminoacyl peptidase (uncomplexed)

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