5TGC
Structure of the hetero-trimer of Rtt102-Arp7/9 bound to ATP
Summary for 5TGC
| Entry DOI | 10.2210/pdb5tgc/pdb |
| Descriptor | Actin-related protein 7, Actin-like protein ARP9, Regulator of Ty1 transposition protein 102, ... (5 entities in total) |
| Functional Keywords | chromatin remodeling complexes, actin-related protein, atp-binding site, nuclear actin, structural protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 6 |
| Total formula weight | 254243.40 |
| Authors | Turegun, B.,Dominguez, R. (deposition date: 2016-09-27, release date: 2017-09-06, Last modification date: 2023-10-04) |
| Primary citation | Turegun, B.,Baker, R.W.,Leschziner, A.E.,Dominguez, R. Actin-related proteins regulate the RSC chromatin remodeler by weakening intramolecular interactions of the Sth1 ATPase. Commun Biol, 1:-, 2018 Cited by PubMed Abstract: The catalytic subunits of SWI/SNF-family and INO80-family chromatin remodelers bind actin and actin-related proteins (Arps) through an N-terminal helicase/SANT-associated (HSA) domain. Between the HSA and ATPase domains lies a conserved post-HSA (pHSA) domain. The HSA domain of Sth1, the catalytic subunit of the yeast SWI/SNF-family remodeler RSC, recruits the Rtt102-Arp7/9 heterotrimer. Rtt102-Arp7/9 regulates RSC function, but the mechanism is unclear. We show that the pHSA domain interacts directly with another conserved region of the catalytic subunit, protrusion-1. Rtt102-Arp7/9 binding to the HSA domain weakens this interaction and promotes the formation of stable, monodisperse complexes with DNA and nucleosomes. A crystal structure of Rtt102-Arp7/9 shows that ATP binds to Arp7 but not Arp9. However, Arp7 does not hydrolyze ATP. Together, the results suggest that Rtt102 and ATP stabilize a conformation of Arp7/9 that potentiates binding to the HSA domain, which releases intramolecular interactions within Sth1 and controls DNA and nucleosome binding. PubMed: 29809203DOI: 10.1038/s42003-017-0002-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.245 Å) |
Structure validation
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