4nl8: Difference between revisions
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==PriA Helicase Bound to SSB C-terminal Tail Peptide== | |||
<StructureSection load='4nl8' size='340' side='right' caption='[[4nl8]], [[Resolution|resolution]] 4.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4nl8]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Klep7 Klep7] and [http://en.wikipedia.org/wiki/Kleph Kleph]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NL8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2d7g|2d7g]], [[2d7h|2d7h]], [[2dwl|2dwl]], [[2dwm|2dwm]], [[2dwn|2dwn]], [[2d7e|2d7e]], [[4nl4|4nl4]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KPHS_02830, ssb c-terminal peptide ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1125630 KLEPH]), KPN78578_41850, KPN_04230, priA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272620 KLEP7])</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=4nl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nl8 RCSB], [http://www.ebi.ac.uk/pdbsum/4nl8 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Collisions between cellular DNA replication machinery (replisomes) and damaged DNA or immovable protein complexes can dissociate replisomes before the completion of replication. This potentially lethal problem is resolved by cellular "replication restart" reactions that recognize the structures of prematurely abandoned replication forks and mediate replisomal reloading. In bacteria, this essential activity is orchestrated by the PriA DNA helicase, which identifies replication forks via structure-specific DNA binding and interactions with fork-associated ssDNA-binding proteins (SSBs). However, the mechanisms by which PriA binds replication fork DNA and coordinates subsequent replication restart reactions have remained unclear due to the dearth of high-resolution structural information available for the protein. Here, we describe the crystal structures of full-length PriA and PriA bound to SSB. The structures reveal a modular arrangement for PriA in which several DNA-binding domains surround its helicase core in a manner that appears to be poised for binding to branched replication fork DNA structures while simultaneously allowing complex formation with SSB. PriA interaction with SSB is shown to modulate SSB/DNA complexes in a manner that exposes a potential replication initiation site. From these observations, a model emerges to explain how PriA links recognition of diverse replication forks to replication restart. | |||
Structural mechanisms of PriA-mediated DNA replication restart.,Bhattacharyya B, George NP, Thurmes TM, Zhou R, Jani N, Wessel SR, Sandler SJ, Ha T, Keck JL Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):1373-8. doi:, 10.1073/pnas.1318001111. Epub 2013 Dec 30. PMID:24379377<ref>PMID:24379377</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Bhattacharyya, B | == References == | ||
[[Category: George, N P | <references/> | ||
[[Category: Keck, J L | __TOC__ | ||
[[Category: Thurmes, T M | </StructureSection> | ||
[[Category: Klep7]] | |||
[[Category: Kleph]] | |||
[[Category: Bhattacharyya, B]] | |||
[[Category: George, N P]] | |||
[[Category: Keck, J L]] | |||
[[Category: Thurmes, T M]] | |||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Helicase]] | [[Category: Helicase]] | ||
Revision as of 19:55, 21 December 2014
PriA Helicase Bound to SSB C-terminal Tail PeptidePriA Helicase Bound to SSB C-terminal Tail Peptide
Structural highlights
Publication Abstract from PubMedCollisions between cellular DNA replication machinery (replisomes) and damaged DNA or immovable protein complexes can dissociate replisomes before the completion of replication. This potentially lethal problem is resolved by cellular "replication restart" reactions that recognize the structures of prematurely abandoned replication forks and mediate replisomal reloading. In bacteria, this essential activity is orchestrated by the PriA DNA helicase, which identifies replication forks via structure-specific DNA binding and interactions with fork-associated ssDNA-binding proteins (SSBs). However, the mechanisms by which PriA binds replication fork DNA and coordinates subsequent replication restart reactions have remained unclear due to the dearth of high-resolution structural information available for the protein. Here, we describe the crystal structures of full-length PriA and PriA bound to SSB. The structures reveal a modular arrangement for PriA in which several DNA-binding domains surround its helicase core in a manner that appears to be poised for binding to branched replication fork DNA structures while simultaneously allowing complex formation with SSB. PriA interaction with SSB is shown to modulate SSB/DNA complexes in a manner that exposes a potential replication initiation site. From these observations, a model emerges to explain how PriA links recognition of diverse replication forks to replication restart. Structural mechanisms of PriA-mediated DNA replication restart.,Bhattacharyya B, George NP, Thurmes TM, Zhou R, Jani N, Wessel SR, Sandler SJ, Ha T, Keck JL Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):1373-8. doi:, 10.1073/pnas.1318001111. Epub 2013 Dec 30. PMID:24379377[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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