4bxf: Difference between revisions

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==60S ribosomal protein L27A histidine hydroxylase (MINA53 Y209C) in complex with MN(II), 2-oxoglutarate (2OG) and 60S ribosomal protein L27A (RPL27A G37C) peptide fragment==
==60S ribosomal protein L27A histidine hydroxylase (MINA53 Y209C) in complex with MN(II), 2-oxoglutarate (2OG) and 60S ribosomal protein L27A (RPL27A G37C) peptide fragment==
<StructureSection load='4bxf' size='340' side='right' caption='[[4bxf]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='4bxf' size='340' side='right'caption='[[4bxf]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4bxf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BXF FirstGlance]. <br>
<table><tr><td colspan='2'>[[4bxf]] 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=4BXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BXF FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xdv|2xdv]], [[4bu2|4bu2]], [[4ccj|4ccj]], [[4cck|4cck]], [[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=AKG:2-OXOGLUTARIC+ACID'>AKG</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bxf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bxf RCSB], [http://www.ebi.ac.uk/pdbsum/4bxf PDBsum]</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=4bxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bxf OCA], [https://pdbe.org/4bxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bxf RCSB], [https://www.ebi.ac.uk/pdbsum/4bxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bxf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MINA_HUMAN MINA_HUMAN]] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.<ref>PMID:12091391</ref> <ref>PMID:15897898</ref> <ref>PMID:14695334</ref> <ref>PMID:15534111</ref> <ref>PMID:15819408</ref> <ref>PMID:17317935</ref> <ref>PMID:19502796</ref> <ref>PMID:23103944</ref>
[https://www.uniprot.org/uniprot/RIOX2_HUMAN RIOX2_HUMAN] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.<ref>PMID:12091391</ref> <ref>PMID:14695334</ref> <ref>PMID:15534111</ref> <ref>PMID:15819408</ref> <ref>PMID:15897898</ref> <ref>PMID:17317935</ref> <ref>PMID:19502796</ref> <ref>PMID:23103944</ref>  
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4bxf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chowdhury, R]]
[[Category: Homo sapiens]]
[[Category: Schofield, C J]]
[[Category: Large Structures]]
[[Category: Beta-hydroxylation]]
[[Category: Chowdhury R]]
[[Category: Dioxygenase]]
[[Category: Schofield CJ]]
[[Category: Dsbh]]
[[Category: Iron-binding]]
[[Category: Jmjc domain]]
[[Category: Non-heme]]
[[Category: Nuclear protein]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-translation complex]]
[[Category: Ribosome biogenesis]]
[[Category: Signaling]]
[[Category: Transcription and epigenetic regulation]]