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| | ==PriA Helicase Bound to SSB C-terminal Tail Peptide== | | ==PriA Helicase Bound to SSB C-terminal Tail Peptide== |
| - | <StructureSection load='4nl8' size='340' side='right' caption='[[4nl8]], [[Resolution|resolution]] 4.08Å' scene=''> | + | <StructureSection load='4nl8' size='340' side='right'caption='[[4nl8]], [[Resolution|resolution]] 4.08Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <table><tr><td colspan='2'>[[4nl8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_subsp._pneumoniae_HS11286 Klebsiella pneumoniae subsp. pneumoniae HS11286] and [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_subsp._pneumoniae_MGH_78578 Klebsiella pneumoniae subsp. pneumoniae MGH 78578]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nl8 OCA], [https://pdbe.org/4nl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nl8 RCSB], [https://www.ebi.ac.uk/pdbsum/4nl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nl8 ProSAT]</span></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://pdbe.org/4nl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nl8 RCSB], [http://www.ebi.ac.uk/pdbsum/4nl8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nl8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H3GL04_KLEPH A0A0H3GL04_KLEPH] Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.[HAMAP-Rule:MF_00984] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Klep7]] | + | [[Category: Klebsiella pneumoniae subsp. pneumoniae HS11286]] |
| - | [[Category: Kleph]] | + | [[Category: Klebsiella pneumoniae subsp. pneumoniae MGH 78578]] |
| - | [[Category: Bhattacharyya, B]] | + | [[Category: Large Structures]] |
| - | [[Category: George, N P]] | + | [[Category: Bhattacharyya B]] |
| - | [[Category: Keck, J L]] | + | [[Category: George NP]] |
| - | [[Category: Thurmes, T M]] | + | [[Category: Keck JL]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Thurmes TM]] |
| - | [[Category: Helicase]]
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| - | [[Category: Pria]]
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| - | [[Category: Reca fold]]
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| - | [[Category: Ssb c-terminal peptide]]
| + | |
| - | [[Category: Winged helix domain]]
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| Structural highlights
Function
A0A0H3GL04_KLEPH Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.[HAMAP-Rule:MF_00984]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bhattacharyya B, George NP, Thurmes TM, Zhou R, Jani N, Wessel SR, Sandler SJ, Ha T, Keck JL. Structural mechanisms of PriA-mediated DNA replication restart. 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 doi:http://dx.doi.org/10.1073/pnas.1318001111
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