2w2i

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(New page: '''Unreleased structure''' The entry 2w2i is ON HOLD Authors: Yue, W.W., Ng, S., Ugochukwu, E., McDonough, M., Pike, A.C.W., Filippakopoulos, P., von Delft, F., Arrowsmith, C., Weigelt,...)
Current revision (15:41, 13 December 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2w2i is ON HOLD
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==Crystal structure of the human 2-oxoglutarate oxygenase LOC390245==
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<StructureSection load='2w2i' size='340' side='right'caption='[[2w2i]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2w2i]] is a 3 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=2W2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W2I FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PD2:PYRIDINE-2,4-DICARBOXYLIC+ACID'>PD2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w2i OCA], [https://pdbe.org/2w2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w2i RCSB], [https://www.ebi.ac.uk/pdbsum/2w2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w2i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KDM4E_HUMAN KDM4E_HUMAN] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code.<ref>PMID:21914792</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w2/2w2i_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2w2i ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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N(epsilon)-Methylations of histone lysine residues play critical roles in cell biology by "marking" chromatin for transcriptional activation or repression. Lysine demethylases reverse N(epsilon)-methylation in a sequence- and methylation-selective manner. The determinants of sequence selectivity for histone demethylases have been unclear. The human JMJD2 (KDM4) H3K9 and H3K36 demethylases can be divided into members that act on both H3K9 and H3K36 and H3K9 alone. Kinetic, crystallographic, and mutagenetic studies in vitro and in cells on KDM4A-E reveal that selectivity is determined by multiple interactions within the catalytic domain but outside the active site. Structurally informed phylogenetic analyses reveal that KDM4A-C orthologues exist in all genome-sequenced vertebrates with earlier animals containing only a single KDM4 enzyme. KDM4D orthologues only exist in eutherians (placental mammals) where they are conserved, including proposed substrate sequence-determining residues. The results will be useful for the identification of inhibitors for specific histone demethylases.
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Authors: Yue, W.W., Ng, S., Ugochukwu, E., McDonough, M., Pike, A.C.W., Filippakopoulos, P., von Delft, F., Arrowsmith, C., Weigelt, J., Edwards, A., Bountra, C., Schofield, C., Oppermann, U.
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Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family.,Hillringhaus L, Yue WW, Rose NR, Ng SS, Gileadi C, Loenarz C, Bello SH, Bray JE, Schofield CJ, Oppermann U J Biol Chem. 2011 Dec 2;286(48):41616-25. Epub 2011 Sep 13. PMID:21914792<ref>PMID:21914792</ref>
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Description: Crystal structure of the human protein LOC390245
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Nov 20 07:35:10 2008''
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<div class="pdbe-citations 2w2i" 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: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith C]]
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[[Category: Bountra C]]
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[[Category: Edwards A]]
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[[Category: Filippakopoulos P]]
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[[Category: McDonough M]]
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[[Category: Ng S]]
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[[Category: Oppermann U]]
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[[Category: Pike ACW]]
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[[Category: Schofield C]]
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[[Category: Shafqat N]]
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[[Category: Ugochukwu E]]
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[[Category: Weigelt J]]
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[[Category: Yue WW]]
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[[Category: Von Delft F]]

Current revision

Crystal structure of the human 2-oxoglutarate oxygenase LOC390245

PDB ID 2w2i

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