7d2d: Difference between revisions
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<StructureSection load='7d2d' size='340' side='right'caption='[[7d2d]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='7d2d' size='340' side='right'caption='[[7d2d]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D2D 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]] 1.8Å</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]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=7d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d2d OCA], [https://pdbe.org/7d2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d2d RCSB], [https://www.ebi.ac.uk/pdbsum/7d2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d2d 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=7d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d2d OCA], [https://pdbe.org/7d2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d2d RCSB], [https://www.ebi.ac.uk/pdbsum/7d2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d2d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hsieh W-L]] | [[Category: Hsieh W-L]] | ||
Latest revision as of 16:30, 6 November 2024
Crystal structure of Ixodes scapularis glutaminyl cyclase with a Mn ion bound to the active siteCrystal structure of Ixodes scapularis glutaminyl cyclase with a Mn ion bound to the active site
Structural highlights
Publication Abstract from PubMedProteins 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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