6f4n

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'''Unreleased structure'''
 
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The entry 6f4n is ON HOLD until Paper Publication
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==Human JMJD5 in complex with MN and 2OG.==
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<StructureSection load='6f4n' size='340' side='right' caption='[[6f4n]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6f4n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F4N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F4N FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f4m|6f4m]], [[6f4o|6f4o]], [[6f4p|6f4p]], [[6f4q|6f4q]], [[6f4r|6f4r]], [[6f4s|6f4s]], [[6f4t|6f4t]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/50S_ribosomal_protein_L16_3-hydroxylase 50S ribosomal protein L16 3-hydroxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.47 1.14.11.47] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f4n OCA], [http://pdbe.org/6f4n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f4n RCSB], [http://www.ebi.ac.uk/pdbsum/6f4n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f4n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/KDM8_HUMAN KDM8_HUMAN]] Histone demethylase required for G2/M phase cell cycle progression. Specifically demethylates dimethylated 'Lys-36' (H3K36me2) of histone H3, an epigenetic repressive mark, thereby acting as a transcription activator. Regulates expression of CCNA1 (cyclin-A1), leading to regulate cancer cell proliferation.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Oxygenase-catalysed post-translational modifications of basic protein residues, including lysyl hydroxylations and N(epsilon)-methyl lysyl demethylations, have important cellular roles. Jumonji-C (JmjC) domain-containing protein 5 (JMJD5), which genetic studies reveal is essential in animal development, is reported as a histone N(epsilon)-methyl lysine demethylase (KDM). Here we report how extensive screening with peptides based on JMJD5 interacting proteins led to the finding that JMJD5 catalyses stereoselective C-3 hydroxylation of arginine residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6). High-resolution crystallographic analyses reveal overall fold, active site and substrate binding/product release features supporting the assignment of JMJD5 as an arginine hydroxylase rather than a KDM. The results will be useful in the development of selective oxygenase inhibitors for the treatment of cancer and genetic diseases.
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Authors:
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JMJD5 is a human arginyl C-3 hydroxylase.,Wilkins SE, Islam S, Gannon JM, Markolovic S, Hopkinson RJ, Ge W, Schofield CJ, Chowdhury R Nat Commun. 2018 Mar 21;9(1):1180. doi: 10.1038/s41467-018-03410-w. PMID:29563586<ref>PMID:29563586</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6f4n" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: 50S ribosomal protein L16 3-hydroxylase]]
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[[Category: Chowdhury, R]]
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[[Category: Islam, M S]]
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[[Category: Schofield, C J]]
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[[Category: 2-oxoglutarate]]
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[[Category: 40s ribosomal protein s6]]
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[[Category: Arginine hydroxylation]]
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[[Category: Arginyl c-3 hydroxylase]]
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[[Category: Beta-hydroxylation]]
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[[Category: Cancer]]
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[[Category: Cell structure]]
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[[Category: Cytoplasm]]
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[[Category: Development]]
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[[Category: Dioxygenase]]
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[[Category: Dna-binding]]
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[[Category: Dsbh]]
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[[Category: Epigenetic regulation]]
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[[Category: Facial triad]]
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[[Category: Hydroxylation]]
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[[Category: Hypoxia]]
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[[Category: Iron]]
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[[Category: Jmjc]]
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[[Category: Jmjc demethylase]]
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[[Category: Jmjc domain]]
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[[Category: Jmjc domain-containing protein 5]]
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[[Category: Jmjc hydroxylase]]
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[[Category: Jmjd5]]
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[[Category: Kdm]]
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[[Category: Kdm8]]
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[[Category: Lysine-specific demethylase 8]]
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[[Category: Metal-binding]]
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[[Category: Non-heme]]
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[[Category: Oxidoreductase]]
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[[Category: Oxygenase]]
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[[Category: Phosphorylation]]
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[[Category: Polymorphism]]
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[[Category: Post-translational modification]]
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[[Category: Ptm]]
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[[Category: Rcc1 domain-containing protein 1]]
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[[Category: Rccd1]]
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[[Category: Regulator of chromosome condensation]]
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[[Category: Ribosome biogenesis]]
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[[Category: Rps6]]
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[[Category: Signaling]]
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[[Category: Transcription]]
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[[Category: Transcription activator/inhibitor]]
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[[Category: Translation]]

Revision as of 06:01, 4 April 2018

Human JMJD5 in complex with MN and 2OG.

6f4n, resolution 2.54Å

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