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PDBsum entry 2v6z
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References listed in PDB file
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Key reference
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Title
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The solution structure of the amino-Terminal domain of human DNA polymerase epsilon subunit b is homologous to c-Domains of aaa+ proteins.
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Authors
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T.Nuutinen,
H.Tossavainen,
K.Fredriksson,
P.Pirilä,
P.Permi,
H.Pospiech,
J.E.Syvaoja.
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Ref.
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Nucleic Acids Res, 2008,
36,
5102-5110.
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PubMed id
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Abstract
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DNA polymerases alpha, delta and epsilon are large multisubunit complexes that
replicate the bulk of the DNA in the eukaryotic cell. In addition to the
homologous catalytic subunits, these enzymes possess structurally related B
subunits, characterized by a carboxyterminal calcineurin-like and an
aminoproximal oligonucleotide/oligosaccharide binding-fold domain. The B
subunits also share homology with the exonuclease subunit of archaeal DNA
polymerases D. Here, we describe a novel domain specific to the N-terminus of
the B subunit of eukaryotic DNA polymerases epsilon. The N-terminal domain of
human DNA polymerases epsilon (Dpoe2NT) expressed in Escherichia coli was
characterized. Circular dichroism studies demonstrated that Dpoe2NT forms a
stable, predominantly alpha-helical structure. The solution structure of Dpoe2NT
revealed a domain that consists of a left-handed superhelical bundle. Four
helices are arranged in two hairpins and the connecting loops contain short
beta-strand segments that form a short parallel sheet. DALI searches
demonstrated a striking structural similarity of the Dpoe2NT with the
alpha-helical subdomains of ATPase associated with various cellular activity
(AAA+) proteins (the C-domain). Like C-domains, Dpoe2NT is rich in charged amino
acids. The biased distribution of the charged residues is reflected by a
polarization and a considerable dipole moment across the Dpoe2NT. Dpoe2NT
represents the first C-domain fold not associated with an AAA+ protein.
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