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4hxe
From Proteopedia
(Difference between revisions)
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| - | + | ==Pyrococcus horikoshii acylaminoacyl peptidase (uncomplexed)== | |
| - | ===Pyrococcus horikoshii | + | <StructureSection load='4hxe' size='340' side='right' caption='[[4hxe]], [[Resolution|resolution]] 1.91Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4hxe]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hxf|4hxf]], [[4hxg|4hxg]]</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 Pyrococcus horikoshii OT3])</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://www.rcsb.org/pdb/explore.do?structureId=4hxe RCSB], [http://www.ebi.ac.uk/pdbsum/4hxe PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Acylaminoacyl-peptidase]] | [[Category: Acylaminoacyl-peptidase]] | ||
[[Category: Pyrococcus horikoshii ot3]] | [[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, D K]] |
| - | [[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: Alpha/beta hyrdolase fold]] | ||
[[Category: Beta-propeller]] | [[Category: Beta-propeller]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Self-compartmentalization]] | [[Category: Self-compartmentalization]] | ||
Revision as of 11:39, 20 January 2015
Pyrococcus horikoshii acylaminoacyl peptidase (uncomplexed)
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Categories: Acylaminoacyl-peptidase | Pyrococcus horikoshii ot3 | Domokos, K | Harmat, V | Hornung, B | Kiss-Szeman, A | Menyhard, D K | Naray-Szabo, G | Polgar, L | Radi, K | Szamosi, I | Szeltner, Z | Tichy-Racs, E | Alpha/beta hyrdolase fold | Beta-propeller | Hydrolase | Self-compartmentalization
