2c9o

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[[Image:2c9o.png|left|200px]]
 
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==3D Structure of the human RuvB-like helicase RuvBL1==
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The line below this paragraph, containing "STRUCTURE_2c9o", creates the "Structure Box" on the page.
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<StructureSection load='2c9o' size='340' side='right'caption='[[2c9o]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2c9o]] 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=2C9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9O 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]] 2.2&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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{{STRUCTURE_2c9o| PDB=2c9o | SCENE= }}
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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=2c9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9o OCA], [https://pdbe.org/2c9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9o RCSB], [https://www.ebi.ac.uk/pdbsum/2c9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RUVB1_HUMAN RUVB1_HUMAN] Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.<ref>PMID:11027681</ref> <ref>PMID:14506706</ref> <ref>PMID:11080158</ref> <ref>PMID:14695187</ref> <ref>PMID:14966270</ref> Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage.<ref>PMID:11027681</ref> <ref>PMID:14506706</ref> <ref>PMID:11080158</ref> <ref>PMID:14695187</ref> <ref>PMID:14966270</ref> Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.<ref>PMID:11027681</ref> <ref>PMID:14506706</ref> <ref>PMID:11080158</ref> <ref>PMID:14695187</ref> <ref>PMID:14966270</ref> Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation.<ref>PMID:11027681</ref> <ref>PMID:14506706</ref> <ref>PMID:11080158</ref> <ref>PMID:14695187</ref> <ref>PMID:14966270</ref> May be able to bind plasminogen at cell surface and enhance plasminogen activation.<ref>PMID:11027681</ref> <ref>PMID:14506706</ref> <ref>PMID:11080158</ref> <ref>PMID:14695187</ref> <ref>PMID:14966270</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/c9/2c9o_consurf.spt"</scriptWhenChecked>
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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=2c9o 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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RuvBL1 is an evolutionarily highly conserved eukaryotic protein belonging to the AAA(+)-family of ATPases (ATPase associated with diverse cellular activities). It plays important roles in essential signaling pathways such as the c-Myc and Wnt pathways in chromatin remodeling, transcriptional and developmental regulation, and DNA repair and apoptosis. Herein we present the three-dimensional structure of the selenomethionine variant of human RuvBL1 refined using diffraction data to 2.2A of resolution. The crystal structure of the hexamer is formed of ADP-bound RuvBL1 monomers. The monomers contain three domains, of which the first and the third are involved in ATP binding and hydrolysis. Although it has been shown that ATPase activity of RuvBL1 is needed for several in vivo functions, we could only detect a marginal activity with the purified protein. Structural homology and DNA binding studies demonstrate that the second domain, which is unique among AAA(+) proteins and not present in the bacterial homolog RuvB, is a novel DNA/RNA-binding domain. We were able to demonstrate that RuvBL1 interacted with single-stranded DNA/RNA and double-stranded DNA. The structure of the RuvBL1.ADP complex, combined with our biochemical results, suggest that although RuvBL1 has all the structural characteristics of a molecular motor, even of an ATP-driven helicase, one or more as yet undetermined cofactors are needed for its enzymatic activity.
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===3D STRUCTURE OF THE HUMAN RUVB-LIKE HELICASE RUVBL1===
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Crystal structure of the human AAA+ protein RuvBL1.,Matias PM, Gorynia S, Donner P, Carrondo MA J Biol Chem. 2006 Dec 15;281(50):38918-29. Epub 2006 Oct 23. PMID:17060327<ref>PMID:17060327</ref>
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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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<div class="pdbe-citations 2c9o" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17060327}}, adds the Publication Abstract to the page
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*[[ATPase|ATPase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17060327 is the PubMed ID number.
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*[[Helicase 3D structures|Helicase 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_17060327}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2C9O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9O OCA].
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==Reference==
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Crystal structure of the human AAA+ protein RuvBL1., Matias PM, Gorynia S, Donner P, Carrondo MA, J Biol Chem. 2006 Dec 15;281(50):38918-29. Epub 2006 Oct 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17060327 17060327]
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Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1., Gorynia S, Matias PM, Goncalves S, Coelho R, Lopes G, Thomaz M, Huber M, Haendler B, Donner P, Carrondo MA, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jan 1;62(Pt, 1):61-6. Epub 2005 Dec 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511264 16511264]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Carrondo, M A.]]
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[[Category: Carrondo MA]]
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[[Category: Donner, P.]]
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[[Category: Donner P]]
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[[Category: Gorynia, S.]]
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[[Category: Gorynia S]]
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[[Category: Matias, P M.]]
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[[Category: Matias PM]]
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[[Category: Aaa+-atpase]]
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[[Category: Activator]]
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[[Category: Atp-binding]]
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[[Category: Chromatin regulator]]
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[[Category: Dna recombination]]
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[[Category: Growth regulation]]
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[[Category: Helicase]]
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[[Category: Hexameric helicase]]
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[[Category: Hydrolase]]
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[[Category: Nuclear protein]]
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[[Category: Nucleotide-binding]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:56:15 2008''
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Current revision

3D Structure of the human RuvB-like helicase RuvBL1

PDB ID 2c9o

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