1rxv: Difference between revisions
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|PDB= 1rxv |SIZE=350|CAPTION= <scene name='initialview01'>1rxv</scene>, resolution 2.5Å | |PDB= 1rxv |SIZE=350|CAPTION= <scene name='initialview01'>1rxv</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= FEN, AF0264 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus]) | |GENE= FEN, AF0264 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1rwz|1RWZ]], [[1rxq|1RXQ]], [[1rxw|1RXW]], [[1rxz|1RXZ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxv OCA], [http://www.ebi.ac.uk/pdbsum/1rxv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rxv RCSB]</span> | |||
}} | }} | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:34:29 2008'' | ||
Revision as of 23:34, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | FEN, AF0264 (Archaeoglobus fulgidus) | ||||||
| Related: | 1RWZ, 1RXQ, 1RXW, 1RXZ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of A. Fulgidus FEN-1 bound to DNA
OverviewOverview
Flap EndoNuclease-1 (FEN-1) and the processivity factor proliferating cell nuclear antigen (PCNA) are central to DNA replication and repair. To clarify the molecular basis of FEN-1 specificity and PCNA activation, we report here structures of FEN-1:DNA and PCNA:FEN-1-peptide complexes, along with fluorescence resonance energy transfer (FRET) and mutational results. FEN-1 binds the unpaired 3' DNA end (3' flap), opens and kinks the DNA, and promotes conformational closing of a flexible helical clamp to facilitate 5' cleavage specificity. Ordering of unstructured C-terminal regions in FEN-1 and PCNA creates an intermolecular beta sheet interface that directly links adjacent PCNA and DNA binding regions of FEN-1 and suggests how PCNA stimulates FEN-1 activity. The DNA and protein conformational changes, composite complex structures, FRET, and mutational results support enzyme-PCNA alignments and a kinked DNA pivot point that appear suitable to coordinate rotary handoffs of kinked DNA intermediates among enzymes localized by the three PCNA binding sites.
About this StructureAbout this Structure
1RXV is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair., Chapados BR, Hosfield DJ, Han S, Qiu J, Yelent B, Shen B, Tainer JA, Cell. 2004 Jan 9;116(1):39-50. PMID:14718165
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