2xdv

From Proteopedia

(Difference between revisions)

Revision as of 20:40, 25 December 2014

Crystal Structure of the Catalytic Domain of FLJ14393

Structural highlights

2xdv is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

2-Oxoglutarate (2OG)-dependent oxygenases have important roles in the regulation of gene expression via demethylation of N-methylated chromatin components and in the hydroxylation of transcription factors and splicing factor proteins. Recently, 2OG-dependent oxygenases that catalyse hydroxylation of transfer RNA and ribosomal proteins have been shown to be important in translation relating to cellular growth, TH17-cell differentiation and translational accuracy. The finding that ribosomal oxygenases (ROXs) occur in organisms ranging from prokaryotes to humans raises questions as to their structural and evolutionary relationships. In Escherichia coli, YcfD catalyses arginine hydroxylation in the ribosomal protein L16; in humans, MYC-induced nuclear antigen (MINA53; also known as MINA) and nucleolar protein 66 (NO66) catalyse histidine hydroxylation in the ribosomal proteins RPL27A and RPL8, respectively. The functional assignments of ROXs open therapeutic possibilities via either ROX inhibition or targeting of differentially modified ribosomes. Despite differences in the residue and protein selectivities of prokaryotic and eukaryotic ROXs, comparison of the crystal structures of E. coli YcfD and Rhodothermus marinus YcfD with those of human MINA53 and NO66 reveals highly conserved folds and novel dimerization modes defining a new structural subfamily of 2OG-dependent oxygenases. ROX structures with and without their substrates support their functional assignments as hydroxylases but not demethylases, and reveal how the subfamily has evolved to catalyse the hydroxylation of different residue side chains of ribosomal proteins. Comparison of ROX crystal structures with those of other JmjC-domain-containing hydroxylases, including the hypoxia-inducible factor asparaginyl hydroxylase FIH and histone Nepsilon-methyl lysine demethylases, identifies branch points in 2OG-dependent oxygenase evolution and distinguishes between JmjC-containing hydroxylases and demethylases catalysing modifications of translational and transcriptional machinery. The structures reveal that new protein hydroxylation activities can evolve by changing the coordination position from which the iron-bound substrate-oxidizing species reacts. This coordination flexibility has probably contributed to the evolution of the wide range of reactions catalysed by oxygenases.

Ribosomal oxygenases are structurally conserved from prokaryotes to humans.,Chowdhury R, Sekirnik R, Brissett NC, Krojer T, Ho CH, Ng SS, Clifton IJ, Ge W, Kershaw NJ, Fox GC, Muniz JR, Vollmar M, Phillips C, Pilka ES, Kavanagh KL, von Delft F, Oppermann U, McDonough MA, Doherty AJ, Schofield CJ Nature. 2014 May 11. doi: 10.1038/nature13263. PMID:24814345^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tsuneoka M, Koda Y, Soejima M, Teye K, Kimura H. A novel myc target gene, mina53, that is involved in cell proliferation. J Biol Chem. 2002 Sep 20;277(38):35450-9. Epub 2002 Jun 28. PMID:12091391 doi:10.1074/jbc.M204458200
↑ Zhang Y, Lu Y, Yuan BZ, Castranova V, Shi X, Stauffer JL, Demers LM, Chen F. The Human mineral dust-induced gene, mdig, is a cell growth regulating gene associated with lung cancer. Oncogene. 2005 Jul 21;24(31):4873-82. PMID:15897898 doi:1208668
↑ Teye K, Tsuneoka M, Arima N, Koda Y, Nakamura Y, Ueta Y, Shirouzu K, Kimura H. Increased expression of a Myc target gene Mina53 in human colon cancer. Am J Pathol. 2004 Jan;164(1):205-16. PMID:14695334
↑ Tsuneoka M, Fujita H, Arima N, Teye K, Okamura T, Inutsuka H, Koda Y, Shirouzu K, Kimura H. Mina53 as a potential prognostic factor for esophageal squamous cell carcinoma. Clin Cancer Res. 2004 Nov 1;10(21):7347-56. PMID:15534111 doi:10/21/7347
↑ Eilbracht J, Kneissel S, Hofmann A, Schmidt-Zachmann MS. Protein NO52--a constitutive nucleolar component sharing high sequence homologies to protein NO66. Eur J Cell Biol. 2005 Mar;84(2-3):279-94. PMID:15819408
↑ Kuratomi K, Yano H, Tsuneoka M, Sakamoto K, Kusukawa J, Kojiro M. Immunohistochemical expression of Mina53 and Ki67 proteins in human primary gingival squamous cell carcinoma. Kurume Med J. 2006;53(3-4):71-8. PMID:17317935
↑ Lu Y, Chang Q, Zhang Y, Beezhold K, Rojanasakul Y, Zhao H, Castranova V, Shi X, Chen F. Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3. Cell Cycle. 2009 Jul 1;8(13):2101-9. Epub 2009 Jul 5. PMID:19502796
↑ Ge W, Wolf A, Feng T, Ho CH, Sekirnik R, Zayer A, Granatino N, Cockman ME, Loenarz C, Loik ND, Hardy AP, Claridge TD, Hamed RB, Chowdhury R, Gong L, Robinson CV, Trudgian DC, Jiang M, Mackeen MM, McCullagh JS, Gordiyenko Y, Thalhammer A, Yamamoto A, Yang M, Liu-Yi P, Zhang Z, Schmidt-Zachmann M, Kessler BM, Ratcliffe PJ, Preston GM, Coleman ML, Schofield CJ. Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans. Nat Chem Biol. 2012 Dec;8(12):960-2. doi: 10.1038/nchembio.1093. Epub 2012 Oct, 28. PMID:23103944 doi:10.1038/nchembio.1093
↑ Chowdhury R, Sekirnik R, Brissett NC, Krojer T, Ho CH, Ng SS, Clifton IJ, Ge W, Kershaw NJ, Fox GC, Muniz JR, Vollmar M, Phillips C, Pilka ES, Kavanagh KL, von Delft F, Oppermann U, McDonough MA, Doherty AJ, Schofield CJ. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature. 2014 May 11. doi: 10.1038/nature13263. PMID:24814345 doi:http://dx.doi.org/10.1038/nature13263

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xdv"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2xdv]] is a 1 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=2XDV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XDV FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xdv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xdv RCSB], [http://www.ebi.ac.uk/pdbsum/2xdv PDBsum]</span></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=2xdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xdv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xdv RCSB], [http://www.ebi.ac.uk/pdbsum/2xdv PDBsum]</span></td></tr>
-<table>
+</table>
+== 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 31: @@
 </StructureSection>
 [[Category: Human]]
-[[Category: Arrowsmith, C H.]]
+[[Category: Arrowsmith, C H]]
-[[Category: Bountra, C.]]
+[[Category: Bountra, C]]
-[[Category: Bunkoczi, G.]]
+[[Category: Bunkoczi, G]]
-[[Category: Daniel, M.]]
+[[Category: Daniel, M]]
-[[Category: Delft, F von.]]
+[[Category: Delft, F von]]
-[[Category: Edwards, A M.]]
+[[Category: Edwards, A M]]
-[[Category: Fedorov, O.]]
+[[Category: Fedorov, O]]
-[[Category: Filippakopoulos, P.]]
+[[Category: Filippakopoulos, P]]
-[[Category: Gileadi, O.]]
+[[Category: Gileadi, O]]
-[[Category: Guo, K.]]
+[[Category: Guo, K]]
-[[Category: Kavanagh, K L.]]
+[[Category: Kavanagh, K L]]
-[[Category: Knapp, S.]]
+[[Category: Knapp, S]]
-[[Category: Kochan, G.]]
+[[Category: Kochan, G]]
-[[Category: Krojer, T.]]
+[[Category: Krojer, T]]
-[[Category: Muniz, J R.C.]]
+[[Category: Muniz, J R.C]]
-[[Category: Ng, S S.]]
+[[Category: Ng, S S]]
-[[Category: Niesen, F.]]
+[[Category: Niesen, F]]
-[[Category: Oppermann, U.]]
+[[Category: Oppermann, U]]
-[[Category: Pike, A C.W.]]
+[[Category: Pike, A C.W]]
-[[Category: Pilka, E.]]
+[[Category: Pilka, E]]
-[[Category: Savitsky, P.]]
+[[Category: Savitsky, P]]
-[[Category: Sobott, F.]]
+[[Category: Sobott, F]]
-[[Category: Weigelt, J.]]
+[[Category: Weigelt, J]]
-[[Category: Yue, W W.]]
+[[Category: Yue, W W]]
 [[Category: Nuclear protein]]
 [[Category: Ribosome biogenesis]]

2xdv

From Proteopedia

Revision as of 20:40, 25 December 2014

Crystal Structure of the Catalytic Domain of FLJ14393

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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