PDBsum entry 6fhs

DNA binding protein

PDB id: 6fhs

Contents

Protein chains

449 a.a.

439 a.a.

267 a.a.

36 a.a.

103 a.a.

441 a.a.

Ligands

ADP ×6

ATP

PDB id:

6fhs

Name:

DNA binding protein

Title:

Cryoem structure of ino80core

Structure:

Ruvb-like helicase. Chain: a, b, c. Engineered: yes. Ruvb-like helicase. Chain: d, e, f. Engineered: yes. Ino80. Chain: g. Engineered: yes.

Source:

Chaetomium thermophilum var. Thermophilum dsm 1495. Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Cell_line: high five cells (bti-tn-5b1-4). Gene: ctht_0006820. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high five cells (bti-tn-5b1-4).

Authors:

S.Eustermann,K.Schall,D.Kostrewa,M.Strauss,K.Hopfner

Key ref:

S.Eustermann et al. (2018). Structural basis for ATP-dependent chromatin remodelling by the INO80 complex. Nature, 556, 386-390. PubMed id: 29643509 DOI: 10.1038/s41586-018-0029-y

Date:

15-Jan-18 Release date: 25-Apr-18

Protein chains

G0RYI5  (G0RYI5_CHATD) -  RuvB-like helicase from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 462 a.a.

Struc: 449 a.a.

Protein chains

G0RYC2  (G0RYC2_CHATD) -  RuvB-like helicase from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 488 a.a.

Struc: 439 a.a.

Protein chain

No UniProt id for this chain

Struc: 267 a.a.

Protein chain

G0RY01  (G0RY01_CHATD) -  INO80 complex subunit B-like conserved region domain-containing protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 492 a.a.

Struc: 36 a.a.

Protein chain

G0S590  (G0S590_CHATD) -  Vps72/YL1 C-terminal domain-containing protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 219 a.a.

Struc: 103 a.a.

Protein chain

G0S589  (G0S589_CHATD) -  Uncharacterized protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 866 a.a.

Struc: 441 a.a.

Enzyme reactions

• Enzyme class 1: Chains A, B, C, D, E, F: E.C.3.6.4.12 - Dna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

ATP (Bound ligand (Het Group name = ATP) corresponds exactly) + H2O = ADP (Bound ligand (Het Group name = ADP) corresponds exactly) + phosphate + H(+)

• Enzyme class 2: Chains H, I, J: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1038/s41586-018-0029-y

Nature 556:386-390 (2018)

PubMed id: 29643509

Structural basis for ATP-dependent chromatin remodelling by the INO80 complex.

S.Eustermann, K.Schall, D.Kostrewa, K.Lakomek, M.Strauss, M.Moldt, K.P.Hopfner.

ABSTRACT

In the eukaryotic nucleus, DNA is packaged in the form of nucleosomes, each of which comprises about 147 base pairs of DNA wrapped around a histone protein octamer. The position and histone composition of nucleosomes is governed by ATP-dependent chromatin remodellers^1-3 such as the 15-subunit INO80 complex ⁴ . INO80 regulates gene expression, DNA repair and replication by sliding nucleosomes, the exchange of histone H2A.Z with H2A, and the positioning of + 1 and -1 nucleosomes at promoter DNA^5-8. The structures and mechanisms of these remodelling reactions are currently unknown. Here we report the cryo-electron microscopy structure of the evolutionarily conserved core of the INO80 complex from the fungus Chaetomium thermophilum bound to a nucleosome, at a global resolution of 4.3 Å and with major parts at 3.7 Å. The INO80 core cradles one entire gyre of the nucleosome through multivalent DNA and histone contacts. An Rvb1/Rvb2 AAA⁺ ATPase heterohexamer is an assembly scaffold for the complex and acts as a 'stator' for the motor and nucleosome-gripping subunits. The Swi2/Snf2 ATPase motor binds to nucleosomal DNA at superhelical location -6, unwraps approximately 15 base pairs, disrupts the H2A-DNA contacts and is poised to pump entry DNA into the nucleosome. Arp5 and Ies6 bind superhelical locations -2 and -3 to act as a counter grip for the motor, on the other side of the H2A-H2B dimer. The Arp5 insertion domain forms a grappler element that binds the nucleosome dyad, connects the Arp5 actin-fold and entry DNA over a distance of about 90 Å and packs against histone H2A-H2B near the 'acidic patch'. Our structure together with biochemical data ⁸ suggests a unified mechanism for nucleosome sliding and histone editing by INO80. The motor is part of a macromolecular ratchet, persistently pumping entry DNA across the H2A-H2B dimer against the Arp5 grip until a large nucleosome translocation step occurs. The transient exposure of H2A-H2B by motor activity as well as differential recognition of H2A.Z and H2A may regulate histone exchange.