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8A5P

Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of Chaetomium thermophilum INO80 on curved DNA

Summary for 8A5P
Entry DOI10.2210/pdb8a5p/pdb
EMDB information15180
DescriptorIno80 ATPase, DNA (36-MER), Actin-related protein 8, ... (9 entities in total)
Functional Keywordschromatin remodeler, ino80, actin-related protein, dna binding protein
Biological sourceThermochaetoides thermophila
More
Total number of polymer chains7
Total formula weight440846.45
Authors
Kunert, F.,Metzner, F.J.,Eustermann, S.,Jung, J.,Woike, S.,Schall, K.,Kostrewa, D.,Hopfner, K.P. (deposition date: 2022-06-15, release date: 2022-12-14, Last modification date: 2024-07-24)
Primary citationKunert, F.,Metzner, F.J.,Jung, J.,Hopfler, M.,Woike, S.,Schall, K.,Kostrewa, D.,Moldt, M.,Chen, J.X.,Bantele, S.,Pfander, B.,Eustermann, S.,Hopfner, K.P.
Structural mechanism of extranucleosomal DNA readout by the INO80 complex.
Sci Adv, 8:eadd3189-eadd3189, 2022
Cited by
PubMed Abstract: The nucleosomal landscape of chromatin depends on the concerted action of chromatin remodelers. The INO80 remodeler specifically places nucleosomes at the boundary of gene regulatory elements, which is proposed to be the result of an ATP-dependent nucleosome sliding activity that is regulated by extranucleosomal DNA features. Here, we use cryo-electron microscopy and functional assays to reveal how INO80 binds and is regulated by extranucleosomal DNA. Structures of the regulatory A-module bound to DNA clarify the mechanism of linker DNA binding. The A-module is connected to the motor unit via an HSA/post-HSA lever element to chemomechanically couple the motor and linker DNA sensing. Two notable sites of curved DNA recognition by coordinated action of the four actin/actin-related proteins and the motor suggest how sliding by INO80 can be regulated by extranucleosomal DNA features. Last, the structures clarify the recruitment of YY1/Ies4 subunits and reveal deep architectural similarities between the regulatory modules of INO80 and SWI/SNF complexes.
PubMed: 36490333
DOI: 10.1126/sciadv.add3189
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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건을2024-11-06부터공개중

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