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==60S ribosomal protein L8 histidine hydroxylase (NO66) in complex with Mn(II) and N-oxalylglycine (NOG)==
==60S ribosomal protein L8 histidine hydroxylase (NO66) in complex with Mn(II) and N-oxalylglycine (NOG)==
<StructureSection load='4cck' size='340' side='right' caption='[[4cck]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='4cck' size='340' side='right'caption='[[4cck]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4cck]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCK FirstGlance]. <br>
<table><tr><td colspan='2'>[[4cck]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CCK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></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]] 2.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xdv|2xdv]], [[4bu2|4bu2]], [[4bxf|4bxf]], [[4ccj|4ccj]], [[4ccm|4ccm]], [[4ccn|4ccn]], [[4cco|4cco]], [[4diq|4diq]]</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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
<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=4cck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cck OCA], [http://pdbe.org/4cck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cck RCSB], [http://www.ebi.ac.uk/pdbsum/4cck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cck 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=4cck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cck OCA], [https://pdbe.org/4cck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cck RCSB], [https://www.ebi.ac.uk/pdbsum/4cck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cck ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NO66_HUMAN NO66_HUMAN]] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>
[https://www.uniprot.org/uniprot/RIOX1_HUMAN RIOX1_HUMAN] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Chowdhury, R]]
[[Category: Large Structures]]
[[Category: Clifton, I J]]
[[Category: Chowdhury R]]
[[Category: Ge, W]]
[[Category: Clifton IJ]]
[[Category: Schofield, C J]]
[[Category: Ge W]]
[[Category: 2-oxoglutarate]]
[[Category: Schofield CJ]]
[[Category: Beta-hydroxylation]]
[[Category: Dioxygenase]]
[[Category: Dsbh]]
[[Category: Iron-binding]]
[[Category: Jmjc domain]]
[[Category: Non-heme]]
[[Category: Nuclear protein]]
[[Category: Oxidoreductase]]
[[Category: Ribosome biogenesis]]
[[Category: Rpl8]]
[[Category: Signaling]]
[[Category: Transcription and epigenetic regulation]]

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