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==Drosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and 2OG== | ==Drosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and 2OG== | ||
<StructureSection load='7yxg' size='340' side='right'caption='[[7yxg]]' scene=''> | <StructureSection load='7yxg' size='340' side='right'caption='[[7yxg]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YXG FirstGlance]. <br> | <table><tr><td colspan='2'>[[7yxg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YXG FirstGlance]. <br> | ||
</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=7yxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yxg OCA], [https://pdbe.org/7yxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yxg RCSB], [https://www.ebi.ac.uk/pdbsum/7yxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yxg ProSAT]</span></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]] 1.641Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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=7yxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yxg OCA], [https://pdbe.org/7yxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yxg RCSB], [https://www.ebi.ac.uk/pdbsum/7yxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yxg ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9VU77_DROME Q9VU77_DROME] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The JmjC family of 2-oxoglutarate dependent oxygenases catalyse a range of hydroxylation and demethylation reactions in humans and other animals. Jumonji domain-containing 7 (JMJD7) is a JmjC (3S)-lysyl-hydroxylase that catalyses the modification of Developmentally Regulated GTP Binding Proteins 1 and 2 (DRG1 and 2); JMJD7 has also been reported to have histone endopeptidase activity. Here we report biophysical and biochemical studies on JMJD7 from Drosophila melanogaster (dmJMJD7). Notably, crystallographic analyses reveal that the unusual dimerization mode of JMJD7, which involves interactions between both the N- and C-terminal regions of both dmJMJD7 monomers and disulfide formation, is conserved in human JMJD7 (hsJMJD7). The results further support the assignment of JMJD7 as a lysyl hydroxylase and will help enable the development of selective inhibitors for it and other JmjC oxygenases. | |||
Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans.,Chowdhury R, Abboud MI, Wiley J, Tumber A, Markolovic S, Schofield CJ Sci Rep. 2022 Apr 11;12(1):6065. doi: 10.1038/s41598-022-10028-y. PMID:35410347<ref>PMID:35410347</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7yxg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chowdhury R]] | [[Category: Chowdhury R]] | ||
[[Category: Schofield CJ]] | [[Category: Schofield CJ]] | ||
Latest revision as of 16:27, 1 February 2024
Drosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and 2OGDrosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and 2OG
Structural highlights
FunctionPublication Abstract from PubMedThe JmjC family of 2-oxoglutarate dependent oxygenases catalyse a range of hydroxylation and demethylation reactions in humans and other animals. Jumonji domain-containing 7 (JMJD7) is a JmjC (3S)-lysyl-hydroxylase that catalyses the modification of Developmentally Regulated GTP Binding Proteins 1 and 2 (DRG1 and 2); JMJD7 has also been reported to have histone endopeptidase activity. Here we report biophysical and biochemical studies on JMJD7 from Drosophila melanogaster (dmJMJD7). Notably, crystallographic analyses reveal that the unusual dimerization mode of JMJD7, which involves interactions between both the N- and C-terminal regions of both dmJMJD7 monomers and disulfide formation, is conserved in human JMJD7 (hsJMJD7). The results further support the assignment of JMJD7 as a lysyl hydroxylase and will help enable the development of selective inhibitors for it and other JmjC oxygenases. Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans.,Chowdhury R, Abboud MI, Wiley J, Tumber A, Markolovic S, Schofield CJ Sci Rep. 2022 Apr 11;12(1):6065. doi: 10.1038/s41598-022-10028-y. PMID:35410347[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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