3wee
From Proteopedia
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(New page: '''Unreleased structure''' The entry 3wee is ON HOLD Authors: Lobsiger, J., Richmond, T.J. Description: Structure of the full-length yeast Arp7/Arp9 Heterodimer) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the full-length yeast Arp7-Arp9 Heterodimer== | |
| + | <StructureSection load='3wee' size='340' side='right'caption='[[3wee]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3wee]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WEE FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMH:S-(METHYLMERCURY)-L-CYSTEINE'>CMH</scene>, <scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3wee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wee OCA], [https://pdbe.org/3wee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wee RCSB], [https://www.ebi.ac.uk/pdbsum/3wee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wee ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ARP9_YEAST ARP9_YEAST] Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP9 and ARP7 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.<ref>PMID:9844636</ref> <ref>PMID:8980231</ref> <ref>PMID:10025404</ref> <ref>PMID:10329629</ref> <ref>PMID:12183366</ref> <ref>PMID:12072455</ref> <ref>PMID:12805231</ref> <ref>PMID:12697820</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The nuclear actin-related proteins Arp7 and Arp9 are components of the yeast SWI/SNF and RSC chromatin-remodelling complexes. The 3.1 A resolution crystal structure reported here shows that the full-length Arp7 and Arp9 proteins exist as a dimer without a requirement for additional polypeptides. Of the 11 actin-related proteins, Arp7 and Arp9 are the only two directly demonstrated to form a dimer within this family. The Arp7-Arp9 heterodimer is unlikely to form an actin-like filament based on modelling using the structure. The Arp7-Arp9 structure reveals that its dimerization interface is not altered when bound in a complex with the SWI/SNF Snf2 HSA domain and the regulatory protein Rtt102. | ||
| - | + | Structure of the full-length yeast Arp7-Arp9 heterodimer.,Lobsiger J, Hunziker Y, Richmond TJ Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):310-6. doi:, 10.1107/S1399004713027417. Epub 2014 Jan 29. PMID:24531465<ref>PMID:24531465</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3wee" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Actin-related protein 3D structures|Actin-related protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Lobsiger J]] | ||
| + | [[Category: Richmond TJ]] | ||
Current revision
Structure of the full-length yeast Arp7-Arp9 Heterodimer
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