7ujl: Difference between revisions

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'''Unreleased structure'''


The entry 7ujl is ON HOLD  until Paper Publication
==Bacteriophage Lambda Red-Beta N-terminal domain helical assembly in complex with dsDNA==
<StructureSection load='7ujl' size='340' side='right'caption='[[7ujl]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ujl]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UJL FirstGlance]. <br>
</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=7ujl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ujl OCA], [https://pdbe.org/7ujl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ujl RCSB], [https://www.ebi.ac.uk/pdbsum/7ujl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ujl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VBET_LAMBD VBET_LAMBD] Gene bet protein functions in general recombination and in the late, rolling-circle mode of lambda DNA replication. Has a function similar to that of E.coli recT. It is a single-stranded DNA binding protein that can promote renaturation of DNA.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Redbeta protein of the bacteriophage lambda red recombination system is a model annealase which catalyzes single-strand annealing homologous DNA recombination. Here we present the structure of a helical oligomeric annealing intermediate of Redbeta, consisting of N-terminal residues 1-177 bound to two complementary 27mer oligonucleotides, determined via cryogenic electron microscopy (cryo-EM) to a final resolution of 3.3 A. The structure reveals a continuous binding groove which positions and stabilizes complementary DNA strands in a planar orientation to facilitate base pairing via a network of hydrogen bonding. Definition of the inter-subunit interface provides a structural basis for the propensity of Redbeta to oligomerize into functionally significant long helical filaments, a trait shared by most annealases. Our cryo-EM structure and molecular dynamics simulations suggest that residues 133-138 form a flexible loop which modulates access to the binding groove. More than half a century after its discovery, this combination of structural and computational observations has allowed us to propose molecular mechanisms for the actions of the model annealase Redbeta, a defining member of the Redbeta/RecT protein family.


Authors:  
Redbeta177 annealase structure reveals details of oligomerization and lambda Red-mediated homologous DNA recombination.,Newing TP, Brewster JL, Fitschen LJ, Bouwer JC, Johnston NP, Yu H, Tolun G Nat Commun. 2022 Sep 26;13(1):5649. doi: 10.1038/s41467-022-33090-6. PMID:36163171<ref>PMID:36163171</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7ujl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia virus Lambda]]
[[Category: Large Structures]]
[[Category: Newing TP]]
[[Category: Tolun GT]]
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