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7d18

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7d18]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidobacteriales_bacterium_59-55 Acidobacteriales bacterium 59-55]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D18 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7d18]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidobacteriales_bacterium_59-55 Acidobacteriales bacterium 59-55]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D18 FirstGlance]. <br>
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</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.332&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BGO25_06485 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1895690 Acidobacteriales bacterium 59-55])</td></tr>
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<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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=7d18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d18 OCA], [https://pdbe.org/7d18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d18 RCSB], [https://www.ebi.ac.uk/pdbsum/7d18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d18 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=7d18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d18 OCA], [https://pdbe.org/7d18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d18 RCSB], [https://www.ebi.ac.uk/pdbsum/7d18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d18 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1Q3QTC5_9BACT A0A1Q3QTC5_9BACT]
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Proteins with sequence or structure similar to those of di-Zn exopeptidases are usually classified as the M28-family enzymes, including the mammalian-type glutaminyl cyclases (QCs). QC catalyzes protein N-terminal pyroglutamate formation, a posttranslational modification important under many physiological and pathological conditions, and is a drug target for treating neurodegenerative diseases, cancers and inflammatory disorders. Without functional characterization, mammalian QCs and their orthologs remain indistinguishable at the sequence and structure levels from other M28-family proteins, leading to few reported QCs. Here, we show that a low-barrier carboxylic-acid hydrogen-bond network (CAHBN) is required for QC activity and discriminates QCs from M28-family peptidases. We demonstrate that the CAHBN-containing M28 peptidases deposited in the PDB are indeed QCs. Our analyses identify several thousands of QCs from the three domains of life, and we enzymatically and structurally characterize several. For the first time, the interplay between a CAHBN and the binuclear metal-binding center of mammalian QCs is made clear. We found that the presence or absence of CAHBN is a key discriminator for the formation of either the mono-Zn QCs or the di-Zn exopeptidases. Our study helps explain the possible roles of QCs in life.
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A unique carboxylic-acid hydrogen-bond network (CAHBN) confers glutaminyl cyclase activity on M28 family enzymes.,Huang KF, Huang JS, Wu ML, Hsieh WL, Hsu KC, Hsu HL, Ko TP, H-J Wang A J Mol Biol. 2021 Mar 24:166960. doi: 10.1016/j.jmb.2021.166960. PMID:33774034<ref>PMID:33774034</ref>
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==See Also==
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*[[Glutaminyl cyclase|Glutaminyl cyclase]]
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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 7d18" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acidobacteriales bacterium 59-55]]
[[Category: Acidobacteriales bacterium 59-55]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hsieh, W L]]
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[[Category: Hsieh W-L]]
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[[Category: Huang, J S]]
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[[Category: Huang J-S]]
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[[Category: Huang, K F]]
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[[Category: Huang K-F]]
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[[Category: Wang, A H.J]]
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[[Category: Wang AH-J]]
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[[Category: Wu, M L]]
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[[Category: Wu M-L]]
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[[Category: Glutaminyl cyclase]]
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[[Category: Metal binding protein]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Acidobacteriales bacterium glutaminyl cyclase

PDB ID 7d18

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