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PDBsum entry 1isq
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DNA binding protein
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PDB id
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1isq
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Physical interaction between proliferating cell nuclear antigen and replication factor c from pyrococcus furiosus.
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Authors
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S.Matsumiya,
S.Ishino,
Y.Ishino,
K.Morikawa.
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Ref.
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Genes Cells, 2002,
7,
911-922.
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PubMed id
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Abstract
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BACKGROUND: Proliferating cell nuclear antigen (PCNA), which is recognized as a
DNA polymerase processivity factor, has direct interactions with various
proteins involved in the important genetic information processes in Eukarya. We
determined the crystal structure of PCNA from the hyperthermophilic archaeon,
Pyrococcus furiosus (PfuPCNA) at 2.1 A resolution, and found that the toroidal
ring-shaped structure, which consists of homotrimeric molecules, is highly
conserved between the Eukarya and Archaea. This allowed us to examine its
interaction with the loading factor at the atomic level. RESULTS: The
replication factor C (RFC) is known as the loading factor of PCNA on to the DNA
strand. P. furiosus RFC (PfuRFC) has a PCNA binding motif (PIP-box) at the
C-terminus of the large subunit (RFCL). An 11 residue-peptide containing a
PIP-box sequence of RFCL inhibited the PCNA-dependent primer extension ability
of P. furiosus PolI in a concentration-dependent manner. To understand the
molecular interaction mechanism of PCNA with PCNA binding proteins, we solved
the crystal structure of PfuPCNA complexed with the PIP-box peptide. The
interaction mode of the two molecules is remarkably similar to that of human
PCNA and a peptide containing the PIP-box of p21(WAF1/CIP1). Moreover, the
PIP-box binding may have some effect on the stability of the ring structure of
PfuPCNA by some domain shift. CONCLUSIONS: Our structural analysis on PfuPCNA
suggests that the interaction mode of the PIP-box with PCNA is generally
conserved among the PCNA interacting proteins and that the functional meaning of
the interaction via the PIP-box possibly depends on each protein. A movement of
the C-terminal region of the PCNA monomer by PIP-box binding may cause the PCNA
ring to be more rigid, suitable for its functions.
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