|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1rxz' size='340' side='right'caption='[[1rxz]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1rxz' size='340' side='right'caption='[[1rxz]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rxz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RXZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rxz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] and [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rwz|1rwz]], [[1rxm|1rxm]], [[1rxv|1rxv]], [[1rxw|1rxw]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCN, AF0335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxz OCA], [https://pdbe.org/1rxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rxz RCSB], [https://www.ebi.ac.uk/pdbsum/1rxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxz ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxz OCA], [http://pdbe.org/1rxz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rxz RCSB], [http://www.ebi.ac.uk/pdbsum/1rxz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PCNA_ARCFU PCNA_ARCFU]] Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication (By similarity). [[http://www.uniprot.org/uniprot/FEN_ARCFU FEN_ARCFU]] Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity). | + | [https://www.uniprot.org/uniprot/PCNA_ARCFU PCNA_ARCFU] Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 37: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arcfl]] | + | [[Category: Archaeoglobus fulgidus]] |
| | + | [[Category: Archaeoglobus fulgidus DSM 4304]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chapados, B R]] | + | [[Category: Chapados BR]] |
| - | [[Category: Han, S]] | + | [[Category: Han S]] |
| - | [[Category: Hosfield, D J]] | + | [[Category: Hosfield DJ]] |
| - | [[Category: Qiu, J]] | + | [[Category: Qiu J]] |
| - | [[Category: Shen, B]] | + | [[Category: Shen B]] |
| - | [[Category: Tainer, J A]] | + | [[Category: Tainer JA]] |
| - | [[Category: Yelent, B]] | + | [[Category: Yelent B]] |
| - | [[Category: Beta-zipper]]
| + | |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Dna replication]]
| + | |
| - | [[Category: Interdomain connecting loop]]
| + | |
| - | [[Category: Replication]]
| + | |
| Structural highlights
Function
PCNA_ARCFU Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chapados BR, Hosfield DJ, Han S, Qiu J, Yelent B, Shen B, Tainer JA. Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell. 2004 Jan 9;116(1):39-50. PMID:14718165
|
