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7d1b

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Current revision (10:52, 27 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7d1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fimbriiglobus_ruber Fimbriiglobus ruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D1B FirstGlance]. <br>
<table><tr><td colspan='2'>[[7d1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fimbriiglobus_ruber Fimbriiglobus ruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D1B 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG5:1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE'>PG5</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]] 1.24&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FRUB_06987 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1908690 Fimbriiglobus ruber])</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG5:1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE'>PG5</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=7d1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d1b OCA], [https://pdbe.org/7d1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d1b RCSB], [https://www.ebi.ac.uk/pdbsum/7d1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d1b 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=7d1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d1b OCA], [https://pdbe.org/7d1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d1b RCSB], [https://www.ebi.ac.uk/pdbsum/7d1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d1b 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/A0A225DNX9_9BACT A0A225DNX9_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 7d1b" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Fimbriiglobus ruber]]
[[Category: Fimbriiglobus ruber]]
[[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 Fimbriiglobus ruber glutaminyl cyclase

PDB ID 7d1b

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