1rxv

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[[Image:1rxv.gif|left|200px]]
 
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==Crystal Structure of A. Fulgidus FEN-1 bound to DNA==
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The line below this paragraph, containing "STRUCTURE_1rxv", creates the "Structure Box" on the page.
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<StructureSection load='1rxv' size='340' side='right'caption='[[1rxv]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rxv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXV FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxv OCA], [https://pdbe.org/1rxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rxv RCSB], [https://www.ebi.ac.uk/pdbsum/1rxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxv ProSAT]</span></td></tr>
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{{STRUCTURE_1rxv| PDB=1rxv | SCENE= }}
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</table>
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== Function ==
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[https://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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/1rxv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rxv ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of A. Fulgidus FEN-1 bound to DNA'''
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==See Also==
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1RXV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXV OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14718165 14718165]
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[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chapados, B R.]]
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[[Category: Chapados BR]]
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[[Category: Han, S.]]
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[[Category: Han S]]
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[[Category: Hosfield, D J.]]
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[[Category: Hosfield DJ]]
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[[Category: Qiu, J.]]
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[[Category: Qiu J]]
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[[Category: Shen, B.]]
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[[Category: Shen B]]
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[[Category: Tainer, J A.]]
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[[Category: Tainer JA]]
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[[Category: Yelent, B.]]
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[[Category: Yelent B]]
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[[Category: 3' flap binding site]]
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[[Category: Dna repair]]
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[[Category: Dna replication]]
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[[Category: Helical clamp]]
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[[Category: Helix-3 turn-helix]]
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[[Category: Protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:02:25 2008''
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Current revision

Crystal Structure of A. Fulgidus FEN-1 bound to DNA

PDB ID 1rxv

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