View source for 7cje


==Structural and kinetic characterization of Porphyromonas gingivalis glutaminyl cyclase==
<StructureSection load='7cje' size='340' side='right'caption='[[7cje]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cje]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis_W83 Porphyromonas gingivalis W83]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CJE 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]] 1.950007&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7cje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cje OCA], [https://pdbe.org/7cje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cje RCSB], [https://www.ebi.ac.uk/pdbsum/7cje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cje ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7MT37_PORGI Q7MT37_PORGI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Porphyromonas gingivalis is a bacterial species known to be involved in the pathogenesis of chronic periodontitis, that more recently has been as well associated with Alzheimer's disease. P. gingivalis expresses a glutaminyl cyclase (PgQC) whose human ortholog is known to participate in the beta amyloid peptide metabolism. We have elucidated the crystal structure of PgQC at 1.95 A resolution in unbound and in inhibitor-complexed forms. The structural characterization of PgQC confirmed that PgQC displays a mammalian fold rather than a bacterial fold. Our biochemical characterization indicates that PgQC uses a mammalian-like catalytic mechanism enabled by the residues Asp(149), Glu(182), Asp(183), Asp(218), Asp(267) and His(299). In addition, we could observe that a non-conserved Trp(193) may drive differences in the binding affinity of ligands which might be useful for drug development. With a screening of a small molecule library, we have identified a benzimidazole derivative rendering PgQC inhibition in the low micromolar range that might be amenable for further medicinal chemistry development.

Structural and kinetic characterization of Porphyromonas gingivalis glutaminyl cyclase.,Lamers S, Feng Q, Cheng Y, Yu S, Sun B, Lukman M, Jiang J, Ruiz-Carrillo D Biol Chem. 2021 Apr 7. pii: hsz-2020-0298. doi: 10.1515/hsz-2020-0298. PMID:33823093<ref>PMID:33823093</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cje" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glutaminyl cyclase|Glutaminyl cyclase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Porphyromonas gingivalis W83]]
[[Category: Feng Q]]
[[Category: Jiang J]]
[[Category: Lamers S]]
[[Category: Lukman M]]
[[Category: Ruiz-Carrillo D]]
[[Category: Sun B]]
[[Category: Yu S]]