5nbl

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'''Unreleased structure'''
 
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The entry 5nbl is ON HOLD until Paper Publication
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==Crystal structure of the Arp4-N-actin(APO-state) heterodimer bound by a nanobody==
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<StructureSection load='5nbl' size='340' side='right' caption='[[5nbl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5nbl]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NBL FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nbm|5nbm]], [[5nbn|5nbn]]</td></tr>
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<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=5nbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbl OCA], [http://pdbe.org/5nbl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nbl RCSB], [http://www.ebi.ac.uk/pdbsum/5nbl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ARP4_YEAST ARP4_YEAST]] Chromatin interaction component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. ARP4 recognizes H2AS128ph (gamma-H2A) and is required for NuA4 complex integrity. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the INO80 complex which remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to gamma-H2A as a response to DNA damage.<ref>PMID:10911987</ref> <ref>PMID:10952318</ref> <ref>PMID:11937627</ref> <ref>PMID:12353039</ref> <ref>PMID:14622406</ref> <ref>PMID:14645854</ref> <ref>PMID:14690608</ref> <ref>PMID:15045029</ref> <ref>PMID:15610740</ref> [[http://www.uniprot.org/uniprot/ACT_YEAST ACT_YEAST]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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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: Eustermann, S]]
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[[Category: Hopfner, K P]]
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[[Category: Knoll, K R]]
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[[Category: Actin-related-protein]]
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[[Category: Chromatin remodeling]]
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[[Category: Hydrolase]]
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[[Category: Ino80]]
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[[Category: Nanobody]]
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[[Category: Nua4]]
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[[Category: Nuclear actin]]
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[[Category: Swr1]]

Revision as of 05:58, 22 August 2018

Crystal structure of the Arp4-N-actin(APO-state) heterodimer bound by a nanobody

5nbl, resolution 2.80Å

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