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PDBsum entry 4c2t
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Hydrolase/DNA
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PDB id
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4c2t
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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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Crystal structure of full length deinococcus radiodurans uvrd in complex with DNA
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Structure:
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DNA helicase ii. Chain: a, b, c, d. Synonym: uvrd. Engineered: yes. DNA strand for28. Chain: m, p. Engineered: yes. DNA strand rev28. Chain: n, o.
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Source:
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Deinococcus radiodurans. Organism_taxid: 1299. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct. Organism_taxid: 32630. Organism_taxid: 32630
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Resolution:
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4.00Å
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R-factor:
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0.248
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R-free:
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0.271
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Authors:
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M.Stelter,S.Acajjaoui,S.Mcsweeney,J.Timmins
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Key ref:
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M.Stelter
et al.
(2013).
Structural and mechanistic insight into DNA unwinding by Deinococcus radiodurans UvrD.
Plos One,
8,
e77364.
PubMed id:
DOI:
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Date:
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20-Aug-13
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Release date:
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30-Oct-13
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PROCHECK
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Headers
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References
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Q9RTI9
(Q9RTI9_DEIRA) -
DNA 3'-5' helicase from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
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Seq:
Struc:
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745 a.a.
650 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-A-G-T-G-C-T-C-G-C-A-G-G-T-C-G-T-A-C-C-T-T-T-T-T
25 bases
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G-G-T-A-C-G-A-C-C-T-G-C-G-A-G-C-A-C-T-G-C-T-T-T-T
25 bases
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G-G-T-A-C-G-A-C-C-T-G-C-G-A-G-C-A-C-T-G-C-T-T-T-T-T
26 bases
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G-C-A-G-T-G-C-T-C-G-C-A-G-G-T-C-G-T-A-C-C-T-T-T-T-T
26 bases
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DOI no:
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Plos One
8:e77364
(2013)
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PubMed id:
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Structural and mechanistic insight into DNA unwinding by Deinococcus radiodurans UvrD.
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M.Stelter,
S.Acajjaoui,
S.McSweeney,
J.Timmins.
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ABSTRACT
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DNA helicases are responsible for unwinding the duplex DNA, a key step in many
biological processes. UvrD is a DNA helicase involved in several DNA repair
pathways. We report here crystal structures of Deinococcus radiodurans UvrD
(drUvrD) in complex with DNA in different nucleotide-free and bound states.
These structures provide us with three distinct snapshots of drUvrD in action
and for the first time trap a DNA helicase undergoing a large-scale spiral
movement around duplexed DNA. Our structural data also improve our understanding
of the molecular mechanisms that regulate DNA unwinding by Superfamily 1A (SF1A)
helicases. Our biochemical data reveal that drUvrD is a DNA-stimulated ATPase,
can translocate along ssDNA in the 3'-5' direction and shows ATP-dependent
3'-5', and surprisingly also, 5'-3' helicase activity. Interestingly, we find
that these translocase and helicase activities of drUvrD are modulated by the
ssDNA binding protein. Analysis of drUvrD mutants indicate that the conserved
β-hairpin structure of drUvrD that functions as a separation pin is critical
for both drUvrD's 3'-5' and 5'-3' helicase activities, whereas the GIG motif of
drUvrD involved in binding to the DNA duplex is essential for the 5'-3' helicase
activity only. These special features of drUvrD may reflect its involvement in a
wide range of DNA repair processes in vivo.
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Links
