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PDBsum entry 4lzd
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PDB id:
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Transferase
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Title:
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Human DNA polymerase mu- apoenzyme
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Structure:
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DNA-directed DNA/RNA polymerase mu. Chain: a. Fragment: polymerase mu loop2 deletion variant, unp residues 132-494. Synonym: pol mu, terminal transferase. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: polm, polmu. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.85Å
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R-factor:
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0.181
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R-free:
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0.228
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Authors:
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A.F.Moon,J.M.Pryor,D.A.Ramsden,T.A.Kunkel,K.Bebenek,L.C.Pedersen
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Key ref:
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A.F.Moon
et al.
(2014).
Sustained active site rigidity during synthesis by human DNA polymerase μ.
Nat Struct Biol,
21,
253-260.
PubMed id:
DOI:
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Date:
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31-Jul-13
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Release date:
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05-Feb-14
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PROCHECK
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Headers
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References
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Q9NP87
(DPOLM_HUMAN) -
DNA-directed DNA/RNA polymerase mu from Homo sapiens
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Seq:
Struc:
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494 a.a.
335 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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Enzyme class:
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E.C.2.7.7.7
- DNA-directed Dna polymerase.
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Reaction:
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
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DNA(n)
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+
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2'-deoxyribonucleoside 5'-triphosphate
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=
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DNA(n+1)
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+
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Nat Struct Biol
21:253-260
(2014)
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PubMed id:
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Sustained active site rigidity during synthesis by human DNA polymerase μ.
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A.F.Moon,
J.M.Pryor,
D.A.Ramsden,
T.A.Kunkel,
K.Bebenek,
L.C.Pedersen.
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ABSTRACT
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DNA polymerase μ (Pol μ) is the only template-dependent human DNA polymerase
capable of repairing double-strand DNA breaks (DSBs) with unpaired 3' ends in
nonhomologous end joining (NHEJ). To probe this function, we structurally
characterized Pol μ's catalytic cycle for single-nucleotide incorporation.
These structures indicate that, unlike other template-dependent DNA polymerases,
Pol μ shows no large-scale conformational changes in protein subdomains, amino
acid side chains or DNA upon dNTP binding or catalysis. Instead, the only major
conformational change is seen earlier in the catalytic cycle, when the flexible
loop 1 region repositions upon DNA binding. Pol μ variants with changes in loop
1 have altered catalytic properties and are partially defective in NHEJ. The
results indicate that specific loop 1 residues contribute to Pol μ's unique
ability to catalyze template-dependent NHEJ of DSBs with unpaired 3' ends.
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Links
