PDBsum entry 6raw

Replication

PDB id: 6raw

Contents

Protein chains

603 a.a.

585 a.a.

608 a.a.

576 a.a.

601 a.a.

631 a.a.

542 a.a.

195 a.a.

171 a.a.

162 a.a.

203 a.a.

DNA/RNA

Ligands

ATP ×3

ADP ×3

PDB id:

6raw

Name:

Replication

Title:

D. Melanogaster cmg-DNA, state 1a

Structure:

DNA replication licensing factor mcm2. Chain: 2. Synonym: minichromosome maintenance 2 protein,dmmcm2. Engineered: yes. DNA replication licensing factor mcm3. Chain: 3. Synonym: minichromosome maintenance 3 protein,dmmcm3. Engineered: yes. DNA replication licensing factor mcm4.

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: mcm2, cg7538. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Gene: mcm3, mcm3-ra, cg4206. Gene: dpa, cg1616. Gene: mcm5, cg4082.

Authors:

P.Eickhoff,F.Martino,A.Costa

Key ref:

P.Eickhoff et al. (2019). Molecular Basis for ATP-Hydrolysis-Driven DNA Translocation by the CMG Helicase of the Eukaryotic Replisome. Cell Rep, 28, 2673. PubMed id: 31484077 DOI: 10.1016/j.celrep.2019.07.104

Date:

08-Apr-19 Release date: 11-Sep-19

Protein chain

P49735  (MCM2_DROME) -  DNA replication licensing factor Mcm2 from Drosophila melanogaster

Seq: 887 a.a.

Struc: 603 a.a.

Protein chain

Q9XYU1  (MCM3_DROME) -  DNA replication licensing factor Mcm3 from Drosophila melanogaster

Seq: 819 a.a.

Struc: 585 a.a.

Protein chain

Q26454  (MCM4_DROME) -  DNA replication licensing factor MCM4 from Drosophila melanogaster

Seq: 866 a.a.

Struc: 608 a.a.

Protein chain

Q9VGW6  (MCM5_DROME) -  DNA replication licensing factor Mcm5 from Drosophila melanogaster

Seq: 733 a.a.

Struc: 576 a.a.

Protein chain

Q9V461  (MCM6_DROME) -  DNA replication licensing factor Mcm6 from Drosophila melanogaster

Seq: 817 a.a.

Struc: 601 a.a.

Protein chain

Q9XYU0  (MCM7_DROME) -  DNA replication licensing factor Mcm7 from Drosophila melanogaster

Seq: 720 a.a.

Struc: 631 a.a.

Protein chain

O96989  (O96989_DROME) -  CDC45L from Drosophila melanogaster

Seq: 575 a.a.

Struc: 542 a.a.

Protein chain

Q9W0I7  (Q9W0I7_DROME) -  DNA replication complex GINS protein PSF1 from Drosophila melanogaster

Seq: 202 a.a.

Struc: 195 a.a.

Protein chain

Q9VQY9  (PSF2_DROME) -  Probable DNA replication complex GINS protein PSF2 from Drosophila melanogaster

Seq: 203 a.a.

Struc: 171 a.a.

Protein chain

Q9W2V7  (Q9W2V7_DROME) -  DNA replication complex GINS protein PSF3 from Drosophila melanogaster

Seq: 212 a.a.

Struc: 162 a.a.

Protein chain

Q9VBI1  (Q9VBI1_DROME) -  DNA replication complex GINS protein SLD5 from Drosophila melanogaster

Seq: 228 a.a.

Struc: 203 a.a.

DNA/RNA chains

A-T-C-G-A-T-C-G-A-T-C-G-A-T-T-T-T-T-T-T-T-T-T-T-T-T 26 bases

T-C-G-A-T-C-G-A-T-C-G-A-T 13 bases

Enzyme reactions

• Enzyme class: Chains 2, 3, 4, 5, 6, 7: 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 + phosphate + H(+)

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

reference

DOI no: 10.1016/j.celrep.2019.07.104

Cell Rep 28:2673 (2019)

PubMed id: 31484077

Molecular Basis for ATP-Hydrolysis-Driven DNA Translocation by the CMG Helicase of the Eukaryotic Replisome.

P.Eickhoff, H.B.Kose, F.Martino, T.Petojevic, F.Abid Ali, J.Locke, N.Tamberg, A.Nans, J.M.Berger, M.R.Botchan, H.Yardimci, A.Costa.

ABSTRACT

In the eukaryotic replisome, DNA unwinding by the Cdc45-MCM-Go-Ichi-Ni-San (GINS) (CMG) helicase requires a hexameric ring-shaped ATPase named minichromosome maintenance (MCM), which spools single-stranded DNA through its central channel. Not all six ATPase sites are required for unwinding; however, the helicase mechanism is unknown. We imaged ATP-hydrolysis-driven translocation of the CMG using cryo-electron microscopy (cryo-EM) and found that the six MCM subunits engage DNA using four neighboring protomers at a time, with ATP binding promoting DNA engagement. Morphing between different helicase states leads us to suggest a non-symmetric hand-over-hand rotary mechanism, explaining the asymmetric requirements of ATPase function around the MCM ring of the CMG. By imaging of a higher-order replisome assembly, we find that the Mrc1-Csm3-Tof1 fork-stabilization complex strengthens the interaction between parental duplex DNA and the CMG at the fork, which might support the coupling between DNA translocation and fork unwinding.