We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

4hxf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 4hxf is ON HOLD Authors: Kiss-Szeman, A., Menyhard, D.K., Tichy-Racs, E., Hornung, B., Radi, K., Szeltner, Z., Domokos, K., Szamosi, I., Naray-Szabo...)
Current revision (03:00, 21 November 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 4hxf is ON HOLD
+
==Acylaminoacyl peptidase in complex with Z-Gly-Gly-Phe-chloromethyl ketone==
 +
<StructureSection load='4hxf' size='340' side='right'caption='[[4hxf]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4hxf]] 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=4HXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HXF 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]] 1.601&#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>, <scene name='pdbligand=Y3A:N-[(BENZYLOXY)CARBONYL]GLYCYL-N-[(2S,3R)-4-CHLORO-3-HYDROXY-1-PHENYLBUTAN-2-YL]GLYCINAMIDE'>Y3A</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=4hxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxf OCA], [https://pdbe.org/4hxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hxf RCSB], [https://www.ebi.ac.uk/pdbsum/4hxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxf 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.
-
Authors: Kiss-Szeman, A., Menyhard, D.K., Tichy-Racs, E., Hornung, B., Radi, K., Szeltner, Z., Domokos, K., Szamosi, I., Naray-Szabo, G., Polgar, L., Harmat, V.
+
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>
-
Description: Acylaminoacyl peptidase in complex with Z-Gly-Gly-Phe-chloromethyl ketone
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4hxf" 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]]

Current revision

Acylaminoacyl peptidase in complex with Z-Gly-Gly-Phe-chloromethyl ketone

PDB ID 4hxf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools