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6i52
From Proteopedia
(Difference between revisions)
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<StructureSection load='6i52' size='340' side='right' caption='[[6i52]], [[Resolution|resolution]] 4.70Å' scene=''> | <StructureSection load='6i52' size='340' side='right' caption='[[6i52]], [[Resolution|resolution]] 4.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6i52]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I52 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6i52]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I52 FirstGlance]. <br> |
| - | </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=6i52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i52 OCA], [http://pdbe.org/6i52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i52 RCSB], [http://www.ebi.ac.uk/pdbsum/6i52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i52 ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RFA3, YJL173C, J0506 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RFA2, BUF1, YNL312W, N0368 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RFA1, BUF2, RPA1, YAR007C, FUN3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=6i52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i52 OCA], [http://pdbe.org/6i52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i52 RCSB], [http://www.ebi.ac.uk/pdbsum/6i52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i52 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RFA3_YEAST RFA3_YEAST]] As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism (By similarity). Stimulates the activity of a cognate strand exchange protein (SEP1). [[http://www.uniprot.org/uniprot/RFA1_YEAST RFA1_YEAST]] Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication. [[http://www.uniprot.org/uniprot/RFA2_YEAST RFA2_YEAST]] Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication. | [[http://www.uniprot.org/uniprot/RFA3_YEAST RFA3_YEAST]] As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism (By similarity). Stimulates the activity of a cognate strand exchange protein (SEP1). [[http://www.uniprot.org/uniprot/RFA1_YEAST RFA1_YEAST]] Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication. [[http://www.uniprot.org/uniprot/RFA2_YEAST RFA2_YEAST]] Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Replication Protein A (RPA), the major eukaryotic single stranded DNA-binding protein, binds to exposed ssDNA to protect it from nucleases, participates in a myriad of nucleic acid transactions and coordinates the recruitment of other important players. RPA is a heterotrimer and coats long stretches of single-stranded DNA (ssDNA). The precise molecular architecture of the RPA subunits and its DNA binding domains (DBDs) during assembly is poorly understood. Using cryo electron microscopy we obtained a 3D reconstruction of the RPA trimerisation core bound with ssDNA ( approximately 55 kDa) at approximately 4.7 A resolution and a dimeric RPA assembly on ssDNA. FRET-based solution studies reveal dynamic rearrangements of DBDs during coordinated RPA binding and this activity is regulated by phosphorylation at S178 in RPA70. We present a structural model on how dynamic DBDs promote the cooperative assembly of multiple RPAs on long ssDNA. | ||
| + | |||
| + | A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA.,Yates LA, Aramayo RJ, Pokhrel N, Caldwell CC, Kaplan JA, Perera RL, Spies M, Antony E, Zhang X Nat Commun. 2018 Dec 21;9(1):5447. doi: 10.1038/s41467-018-07883-7. PMID:30575763<ref>PMID:30575763</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6i52" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
[[Category: Aramayo, R J]] | [[Category: Aramayo, R J]] | ||
[[Category: Yates, L A]] | [[Category: Yates, L A]] | ||
Revision as of 06:23, 2 January 2019
Yeast RPA bound to ssDNA
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