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PDBsum entry 2wwy
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Hydrolase/DNA
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PDB id
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2wwy
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Hydrolase/DNA
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Title:
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Structure of human recq-like helicase in complex with a DNA substrate
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Structure:
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Atp-dependent DNA helicase q1. Chain: a, b. Fragment: residues 49-616. Synonym: recq like DNA helicase, DNA-dependent atpase q1. Engineered: yes. DNA oligo (27bp). Chain: o, q, r, t. Engineered: yes. 5'-d( Da dg dc dg dt dc dg da dg da dt dc dcp)-3'.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: r3-prare2. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.
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Resolution:
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2.90Å
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R-factor:
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0.200
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R-free:
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0.236
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Authors:
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A.C.W.Pike,Y.Zhang,C.Schnecke,A.Chaikuad,T.Krojer,C.D.O.Cooper,F.Von Delft,C.H.Arrowsmith,J.Weigelt,A.Edwards,C.Bountra,O.Gileadi
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Key ref:
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A.C.Pike
et al.
(2015).
Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: insights from DNA complex structures.
Proc Natl Acad Sci U S A,
112,
4286-4291.
PubMed id:
DOI:
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Date:
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30-Oct-09
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Release date:
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29-Dec-09
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PROCHECK
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Headers
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References
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P46063
(RECQ1_HUMAN) -
ATP-dependent DNA helicase Q1 from Homo sapiens
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Seq:
Struc:
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649 a.a.
530 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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C-G-G-T-A
5 bases
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A-G-C-G-T-C-G-A-G-A-T-C-C
13 bases
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T-G-G-A-T-C-T-C-G-A-C-G-C-T-C-T-C-C-C-T
20 bases
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G-G-T
3 bases
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A-G-C-G-T-C-G-A-G-A-T-C
12 bases
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G-A-T-C-T-C-G-A-C-G-C-T-C-T-C-C-C-T
18 bases
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DOI no:
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Proc Natl Acad Sci U S A
112:4286-4291
(2015)
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PubMed id:
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Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: insights from DNA complex structures.
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A.C.Pike,
S.Gomathinayagam,
P.Swuec,
M.Berti,
Y.Zhang,
C.Schnecke,
F.Marino,
F.von Delft,
L.Renault,
A.Costa,
O.Gileadi,
A.Vindigni.
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ABSTRACT
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RecQ helicases are a widely conserved family of ATP-dependent motors with
diverse roles in nearly every aspect of bacterial and eukaryotic genome
maintenance. However, the physical mechanisms by which RecQ helicases recognize
and process specific DNA replication and repair intermediates are largely
unknown. Here, we solved crystal structures of the human RECQ1 helicase in
complexes with tailed-duplex DNA and ssDNA. The structures map the interactions
of the ssDNA tail and the branch point along the helicase and Zn-binding
domains, which, together with reported structures of other helicases, define the
catalytic stages of helicase action. We also identify a strand-separating pin,
which (uniquely in RECQ1) is buttressed by the protein dimer interface. A duplex
DNA-binding surface on the C-terminal domain is shown to play a role in DNA
unwinding, strand annealing, and Holliday junction (HJ) branch migration. We
have combined EM and analytical ultracentrifugation approaches to show that
RECQ1 can form what appears to be a flat, homotetrameric complex and propose
that RECQ1 tetramers are involved in HJ recognition. This tetrameric arrangement
suggests a platform for coordinated activity at the advancing and receding
duplexes of an HJ during branch migration.
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Links
