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==Drosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and succinate== | ==Drosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and succinate== | ||
<StructureSection load='7yxh' size='340' side='right'caption='[[7yxh]]' scene=''> | <StructureSection load='7yxh' size='340' side='right'caption='[[7yxh]], [[Resolution|resolution]] 2.30Å' 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=7YXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YXH FirstGlance]. <br> | <table><tr><td colspan='2'>[[7yxh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YXH 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=7yxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yxh OCA], [https://pdbe.org/7yxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yxh RCSB], [https://www.ebi.ac.uk/pdbsum/7yxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yxh ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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=7yxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yxh OCA], [https://pdbe.org/7yxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yxh RCSB], [https://www.ebi.ac.uk/pdbsum/7yxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yxh ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<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 7yxh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chowdhury R]] | [[Category: Chowdhury, R]] | ||
[[Category: Schofield | [[Category: Schofield, C J]] | ||
[[Category: 2-oxoglutarate]] | |||
[[Category: Cancer]] | |||
[[Category: Development]] | |||
[[Category: Developmentally regulated gtp binding protein]] | |||
[[Category: Dimerisation]] | |||
[[Category: Dioxygenase]] | |||
[[Category: Drg1]] | |||
[[Category: Drg2]] | |||
[[Category: Dsbh]] | |||
[[Category: Facial triad]] | |||
[[Category: Helix-loop-helix-beta]] | |||
[[Category: Hydroxylation]] | |||
[[Category: Hypoxia]] | |||
[[Category: Iron]] | |||
[[Category: Jmjc]] | |||
[[Category: Jmjc demethylase]] | |||
[[Category: Jmjc domain]] | |||
[[Category: Jmjc domain-containing protein 7]] | |||
[[Category: Jmjc hydroxylase]] | |||
[[Category: Jmjd7]] | |||
[[Category: Kdm]] | |||
[[Category: Lysyl hydroxylation]] | |||
[[Category: Metal-binding]] | |||
[[Category: Non-heme]] | |||
[[Category: Nucleic acid- binding]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Oxygenase]] | |||
[[Category: Post-translational modification]] | |||
[[Category: Ptm]] | |||
[[Category: Ribosome biogenesis]] | |||
[[Category: Trafac gtpase]] | |||
[[Category: Translation]] | |||
[[Category: Translation factor]] | |||
Revision as of 16:11, 4 May 2022
Drosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and succinateDrosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and succinate
Structural highlights
Publication 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Large Structures
- Chowdhury, R
- Schofield, C J
- 2-oxoglutarate
- Cancer
- Development
- Developmentally regulated gtp binding protein
- Dimerisation
- Dioxygenase
- Drg1
- Drg2
- Dsbh
- Facial triad
- Helix-loop-helix-beta
- Hydroxylation
- Hypoxia
- Iron
- Jmjc
- Jmjc demethylase
- Jmjc domain
- Jmjc domain-containing protein 7
- Jmjc hydroxylase
- Jmjd7
- Kdm
- Lysyl hydroxylation
- Metal-binding
- Non-heme
- Nucleic acid- binding
- Oxidoreductase
- Oxygenase
- Post-translational modification
- Ptm
- Ribosome biogenesis
- Trafac gtpase
- Translation
- Translation factor