1isq: Difference between revisions

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|PDB= 1isq |SIZE=350|CAPTION= <scene name='initialview01'>1isq</scene>, resolution 2.30&Aring;
|PDB= 1isq |SIZE=350|CAPTION= <scene name='initialview01'>1isq</scene>, resolution 2.30&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1ge8|1GE8]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1isq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1isq OCA], [http://www.ebi.ac.uk/pdbsum/1isq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1isq RCSB]</span>
}}
}}


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[[Category: Matsumiya, S.]]
[[Category: Matsumiya, S.]]
[[Category: Morikawa, K.]]
[[Category: Morikawa, K.]]
[[Category: ACE]]
[[Category: toroidal trimer]]
[[Category: toroidal trimer]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:54:28 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:24:06 2008''

Revision as of 21:24, 30 March 2008

File:1isq.jpg


PDB ID 1isq

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands:
Related: 1GE8


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Pyrococcus furiosus PCNA complexed with RFCL PIP-box peptide


OverviewOverview

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.

About this StructureAbout this Structure

1ISQ is a Protein complex structure of sequences from Pyrococcus furiosus. Full crystallographic information is available from OCA.

ReferenceReference

Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus., Matsumiya S, Ishino S, Ishino Y, Morikawa K, Genes Cells. 2002 Sep;7(9):911-22. PMID:12296822

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