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PDBsum entry 6tux
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DNA binding protein
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PDB id
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6tux
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PDB id:
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| Name: |
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DNA binding protein
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Title:
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Human xpg-DNA, complex 2
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Structure:
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DNA repair protein complementing xp-g cells,DNA repair protein complementing xp-g cells. Chain: a, b. Synonym: DNA excision repair protein ercc-5,xeroderma pigmentosum group g-complementing protein,DNA excision repair protein ercc-5, xeroderma pigmentosum group g-complementing protein. Engineered: yes. DNA (5'-d(p Gp Cp Ap Gp Ap Gp Tp T)-3'). Chain: c, e.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ercc5, ercm2, xpg, xpgc. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.
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Resolution:
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3.10Å
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R-factor:
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0.249
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R-free:
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0.303
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Authors:
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F.M.Ruiz,C.Fernandez-Tornero
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Key ref:
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R.González-Corrochano
et al.
(2020).
The crystal structure of human XPG, the xeroderma pigmentosum group G endonuclease, provides insight into nucleotide excision DNA repair.
Nucleic Acids Res,
48,
9943-9958.
PubMed id:
DOI:
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Date:
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08-Jan-20
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Release date:
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16-Sep-20
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PROCHECK
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Headers
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References
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P28715
(ERCC5_HUMAN) -
DNA excision repair protein ERCC-5 from Homo sapiens
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Seq:
Struc:
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1186 a.a.
330 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 95 residue positions (black
crosses)
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G-C-A-G-A-G-T-T
8 bases
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A-A-C-T-C-T-G-C
8 bases
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A-G-A-G-T-T-C
7 bases
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G-A-A-C-T-C-T
7 bases
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DOI no:
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Nucleic Acids Res
48:9943-9958
(2020)
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PubMed id:
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The crystal structure of human XPG, the xeroderma pigmentosum group G endonuclease, provides insight into nucleotide excision DNA repair.
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R.González-Corrochano,
F.M.Ruiz,
N.M.I.Taylor,
S.Huecas,
S.Drakulic,
M.Spínola-Amilibia,
C.Fernández-Tornero.
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ABSTRACT
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Nucleotide excision repair (NER) is an essential pathway to remove bulky lesions
affecting one strand of DNA. Defects in components of this repair system are at
the ground of genetic diseases such as xeroderma pigmentosum (XP) and Cockayne
syndrome (CS). The XP complementation group G (XPG) endonuclease cleaves the
damaged DNA strand on the 3' side of the lesion coordinated with DNA
re-synthesis. Here, we determined crystal structures of the XPG nuclease domain
in the absence and presence of DNA. The overall fold exhibits similarities to
other flap endonucleases but XPG harbors a dynamic helical arch that is uniquely
oriented and defines a gateway. DNA binding through a helix-2-turn-helix motif,
assisted by one flanking α-helix on each side, shows high plasticity, which is
likely relevant for DNA scanning. A positively-charged canyon defined by the
hydrophobic wedge and β-pin motifs provides an additional DNA-binding surface.
Mutational analysis identifies helical arch residues that play critical roles in
XPG function. A model for XPG participation in NER is proposed. Our structures
and biochemical data represent a valuable tool to understand the atomic ground
of XP and CS, and constitute a starting point for potential therapeutic
applications.
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Links
