7vgc

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Current revision (11:44, 30 October 2024) (edit) (undo)
 
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<StructureSection load='7vgc' size='340' side='right'caption='[[7vgc]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
<StructureSection load='7vgc' size='340' side='right'caption='[[7vgc]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7vgc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microbulbifer_arenaceous Microbulbifer arenaceous]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VGC FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VGC 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]] 2.722&#8491;</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]] 2.722&#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=ZPR:N-BENZYLOXYCARBONYL-L-PROLYL-L-PROLINAL'>ZPR</scene></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=ZPR:N-BENZYLOXYCARBONYL-L-PROLYL-L-PROLINAL'>ZPR</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=7vgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vgc OCA], [https://pdbe.org/7vgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vgc RCSB], [https://www.ebi.ac.uk/pdbsum/7vgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vgc ProSAT]</span></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=7vgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vgc OCA], [https://pdbe.org/7vgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vgc RCSB], [https://www.ebi.ac.uk/pdbsum/7vgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vgc ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Prolyl oligopeptidases (POPs) are atypical serine proteases that are unique in their involvement in the maturation and degradation of prolyl-containing peptide hormones and neuropeptides. They are potential pharmaceutical targets for the treatment of several neurodegenerative disorders, such as Alzheimer's disease. In this study, the catalytic and substrate-regulatory mechanisms of a novel bacterial POP from Microbulbifer arenaceous (MaPOP) were investigated. The crystal structure revealed that the catalytic triad of MaPOP was covered by the central tunnel of an unusual beta-propeller domain. The tunnel not only provided the sole access to the active site for oligopeptides, but also protected large structured peptides or proteins from accidental proteolysis. The enzyme was able to cleave angiotensin I specifically at the carboxyl side of the internal proline residue, but could not hydrolyze long-chain bovine insulin B in vitro. Like the ligand-free structure, MaPOP bound to the transition-state analog inhibitor ZPR was also in a closed state, which was not modulated by the common `latching loop' found in other POPs. The substrate-assisted catalytic mechanism of MaPOP reported here may represent a common mechanism for all POPs. These results may facilitate a better understanding of the catalytic behavior of POPs under physiological conditions.
 
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The structure and molecular dynamics of prolyl oligopeptidase from Microbulbifer arenaceous provide insights into catalytic and regulatory mechanisms.,Huang P, Lv A, Yan Q, Jiang Z, Yang S Acta Crystallogr D Struct Biol. 2022 Jun 1;78(Pt 6):735-751. doi:, 10.1107/S2059798322004247. Epub 2022 May 9. PMID:35647921<ref>PMID:35647921</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 7vgc" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Microbulbifer arenaceous]]
 
[[Category: Huang P]]
[[Category: Huang P]]
[[Category: Jiang ZQ]]
[[Category: Jiang ZQ]]
[[Category: Yang SQ]]
[[Category: Yang SQ]]

Current revision

Crystal structure of prolyl oligopeptidase from Microbulbifer arenaceous complex with a transition state analog inhibitor ZPR

PDB ID 7vgc

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