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PDBsum entry 3qe9
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Hydrolase/DNA
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PDB id
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3qe9
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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 human exonuclease 1 exo1 (d173a) in complex with DNA (complex i)
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Structure:
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Exonuclease 1. Chain: y, z. Synonym: hexo1, exonuclease i, hexoi. Engineered: yes. Mutation: yes. DNA (5'-d( Cp Gp Cp Tp Ap Gp Tp Cp Gp Ap Cp Ap T)-3'). Chain: c, a. Engineered: yes. DNA (5'-d(p Tp Cp Gp Ap Cp Tp Ap Gp Cp G)-3').
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: exo1, exoi, hex1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic: yes
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Resolution:
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2.51Å
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R-factor:
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0.215
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R-free:
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0.238
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Authors:
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J.Orans,E.A.Mcsweeney,R.R.Iyer,M.A.Hast,H.W.Hellinga,P.Modrich, L.S.Beese
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Key ref:
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J.Orans
et al.
(2011).
Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family.
Cell,
145,
212-223.
PubMed id:
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Date:
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20-Jan-11
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Release date:
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20-Apr-11
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PROCHECK
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Headers
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References
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Q9UQ84
(EXO1_HUMAN) -
Exonuclease 1 from Homo sapiens
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Seq:
Struc:
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846 a.a.
345 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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C-G-C-T-A-G-T-C-G-A-C-A-T
13 bases
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T-C-G-A-C-T-A-G-C-G
10 bases
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C-G-C-T-A-G-T-C-G-A-C-A
12 bases
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T-C-G-A-C-T-A-G-C-G
10 bases
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Cell
145:212-223
(2011)
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PubMed id:
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Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family.
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J.Orans,
E.A.McSweeney,
R.R.Iyer,
M.A.Hast,
H.W.Hellinga,
P.Modrich,
L.S.Beese.
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ABSTRACT
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Human exonuclease 1 (hExo1) plays important roles in DNA repair and
recombination processes that maintain genomic integrity. It is a member of the
5' structure-specific nuclease family of exonucleases and endonucleases that
includes FEN-1, XPG, and GEN1. We present structures of hExo1 in complex with a
DNA substrate, followed by mutagenesis studies, and propose a common mechanism
by which this nuclease family recognizes and processes diverse DNA structures.
hExo1 induces a sharp bend in the DNA at nicks or gaps. Frayed 5' ends of nicked
duplexes resemble flap junctions, unifying the mechanisms of endo- and
exonucleolytic processing. Conformational control of a mobile region in the
catalytic site suggests a mechanism for allosteric regulation by binding to
protein partners. The relative arrangement of substrate binding sites in these
enzymes provides an elegant solution to a complex geometrical puzzle of
substrate recognition and processing.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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R.S.Williams,
and
T.A.Kunkel
(2011).
FEN nucleases: bind, bend, fray, cut.
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Cell,
145,
171-172.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
