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5eay: Difference between revisions

New page: ==Crystal structure of a Dna2 peptide in complex with Rpa 70N== <StructureSection load='5eay' size='340' side='right' caption='5eay, resolution 1.55Å' scene=''> ==...
 
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==Crystal structure of a Dna2 peptide in complex with Rpa 70N==
==Crystal structure of a Dna2 peptide in complex with Rpa 70N==
<StructureSection load='5eay' size='340' side='right' caption='[[5eay]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
<StructureSection load='5eay' size='340' side='right'caption='[[5eay]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5eay]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EAY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EAY FirstGlance]. <br>
<table><tr><td colspan='2'>[[5eay]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EAY FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ean|5ean]], [[5eaw|5eaw]], [[5eax|5eax]]</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]] 1.55&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eay OCA], [http://pdbe.org/5eay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eay RCSB], [http://www.ebi.ac.uk/pdbsum/5eay PDBsum]</span></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=5eay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eay OCA], [https://pdbe.org/5eay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eay RCSB], [https://www.ebi.ac.uk/pdbsum/5eay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eay ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/DNA2_HUMAN DNA2_HUMAN]] Mitochondrial DNA deletion syndrome with progressive myopathy. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN]] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>  Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> [[http://www.uniprot.org/uniprot/DNA2_HUMAN DNA2_HUMAN]] Key enzyme involved in DNA replication and DNA repair in nucleus and mitochondrion. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair: recruited by BLM and mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the presence of RPA. Also involved in DNA replication checkpoint independently of Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is subject to debate. According to various reports, the helicase activity is weak and its function remains largely unclear. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function.<ref>PMID:16595799</ref> <ref>PMID:16595800</ref> <ref>PMID:18995831</ref> <ref>PMID:19487465</ref> <ref>PMID:21325134</ref> <ref>PMID:21572043</ref> <ref>PMID:22570407</ref> <ref>PMID:22570476</ref> 
[https://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>  Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
<div class="pdbe-citations 5eay" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5eay" style="background-color:#fffaf0;"></div>
==See Also==
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pavletich, N P]]
[[Category: Homo sapiens]]
[[Category: Pourmal, S]]
[[Category: Large Structures]]
[[Category: Zhou, C]]
[[Category: Pavletich NP]]
[[Category: Dna binding protein]]
[[Category: Pourmal S]]
[[Category: Zhou C]]

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