5NBN
Crystal structure of the Arp4-N-actin-Arp8-Ino80HSA module of INO80
Summary for 5NBN
| Entry DOI | 10.2210/pdb5nbn/pdb |
| Related | 5NBL 5NBM |
| Descriptor | Actin-related protein 4, Actin, Actin-like protein ARP8, ... (7 entities in total) |
| Functional Keywords | chromatin remodeling, nanobody, ino80, swr1, nua4, hydrolase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 8 |
| Total formula weight | 376334.93 |
| Authors | Knoll, K.R.,Eustermann, S.,Hopfner, K.P. (deposition date: 2017-03-02, release date: 2018-08-22, Last modification date: 2024-01-17) |
| Primary citation | Knoll, K.R.,Eustermann, S.,Niebauer, V.,Oberbeckmann, E.,Stoehr, G.,Schall, K.,Tosi, A.,Schwarz, M.,Buchfellner, A.,Korber, P.,Hopfner, K.P. The nuclear actin-containing Arp8 module is a linker DNA sensor driving INO80 chromatin remodeling. Nat. Struct. Mol. Biol., 25:823-832, 2018 Cited by PubMed Abstract: Nuclear actin (N-actin) and actin-related proteins (Arps) are critical components of several chromatin modulating complexes, including the chromatin remodeler INO80, but their function is largely elusive. Here, we report the crystal structure of the 180-kDa Arp8 module of Saccharomyces cerevisiae INO80 and establish its role in recognition of extranucleosomal linker DNA. Arp8 engages N-actin in a manner distinct from that of other actin-fold proteins and thereby specifies recruitment of the Arp4-N-actin heterodimer to a segmented scaffold of the helicase-SANT-associated (HSA) domain of Ino80. The helical HSA domain spans over 120 Å and provides an extended binding platform for extranucleosomal entry DNA that is required for nucleosome sliding and genome-wide nucleosome positioning. Together with the recent cryo-electron microscopy structure of INO80-nucleosome complex, our findings suggest an allosteric mechanism by which INO80 senses 40-bp linker DNA to conduct highly processive chromatin remodeling. PubMed: 30177756DOI: 10.1038/s41594-018-0115-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
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