4zws: Difference between revisions
New page: '''Unreleased structure''' The entry 4zws is ON HOLD until Paper Publication Authors: Gajewski, S., White, S.W. Description: Crystal Structure of the Bacteriophage T4 recombination med... |
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==Crystal Structure of the Bacteriophage T4 recombination mediator protein UvsY, Lattice Type III== | |||
<StructureSection load='4zws' size='340' side='right'caption='[[4zws]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zws]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZWS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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=4zws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zws OCA], [https://pdbe.org/4zws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zws RCSB], [https://www.ebi.ac.uk/pdbsum/4zws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zws ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UVSY_BPT4 UVSY_BPT4] Plays a role in viral DNA synthesis by promoting enzymatic activities of UvsX recombinase, by promoting UvsX-ssDNA filament assembly, and by helping UvsX to displace bound gp32 from ssDNA.<ref>PMID:18565541</ref> <ref>PMID:20371513</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The UvsY recombination mediator protein is critical for efficient homologous recombination in bacteriophage T4 and is the functional analog of the eukaryotic Rad52 protein. During T4 homologous recombination, the UvsX recombinase has to compete with the prebound gp32 single-stranded binding protein for DNA-binding sites and UvsY stimulates this filament nucleation event. We report here the crystal structure of UvsY in four similar open-barrel heptameric assemblies and provide structural and biophysical insights into its function. The UvsY heptamer was confirmed in solution by centrifugation and light scattering, and thermodynamic analyses revealed that the UvsY-ssDNA interaction occurs within the assembly via two distinct binding modes. Using surface plasmon resonance, we also examined the binding of UvsY to both ssDNA and the ssDNA-gp32 complex. These analyses confirmed that ssDNA can bind UvsY and gp32 independently and also as a ternary complex. They also showed that residues located on the rim of the heptamer are required for optimal binding to ssDNA, thus identifying the putative ssDNA-binding surface. We propose a model in which UvsY promotes a helical ssDNA conformation that disfavors the binding of gp32 and initiates the assembly of the ssDNA-UvsX filament. | |||
Structure and mechanism of the phage T4 recombination mediator protein UvsY.,Gajewski S, Waddell MB, Vaithiyalingam S, Nourse A, Li Z, Woetzel N, Alexander N, Meiler J, White SW Proc Natl Acad Sci U S A. 2016 Mar 22;113(12):3275-80. doi:, 10.1073/pnas.1519154113. Epub 2016 Mar 7. PMID:26951671<ref>PMID:26951671</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4zws" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia virus T4]] | |||
[[Category: Large Structures]] | |||
[[Category: Gajewski S]] | |||
[[Category: White SW]] | |||
Latest revision as of 11:25, 27 September 2023
Crystal Structure of the Bacteriophage T4 recombination mediator protein UvsY, Lattice Type IIICrystal Structure of the Bacteriophage T4 recombination mediator protein UvsY, Lattice Type III
Structural highlights
FunctionUVSY_BPT4 Plays a role in viral DNA synthesis by promoting enzymatic activities of UvsX recombinase, by promoting UvsX-ssDNA filament assembly, and by helping UvsX to displace bound gp32 from ssDNA.[1] [2] Publication Abstract from PubMedThe UvsY recombination mediator protein is critical for efficient homologous recombination in bacteriophage T4 and is the functional analog of the eukaryotic Rad52 protein. During T4 homologous recombination, the UvsX recombinase has to compete with the prebound gp32 single-stranded binding protein for DNA-binding sites and UvsY stimulates this filament nucleation event. We report here the crystal structure of UvsY in four similar open-barrel heptameric assemblies and provide structural and biophysical insights into its function. The UvsY heptamer was confirmed in solution by centrifugation and light scattering, and thermodynamic analyses revealed that the UvsY-ssDNA interaction occurs within the assembly via two distinct binding modes. Using surface plasmon resonance, we also examined the binding of UvsY to both ssDNA and the ssDNA-gp32 complex. These analyses confirmed that ssDNA can bind UvsY and gp32 independently and also as a ternary complex. They also showed that residues located on the rim of the heptamer are required for optimal binding to ssDNA, thus identifying the putative ssDNA-binding surface. We propose a model in which UvsY promotes a helical ssDNA conformation that disfavors the binding of gp32 and initiates the assembly of the ssDNA-UvsX filament. Structure and mechanism of the phage T4 recombination mediator protein UvsY.,Gajewski S, Waddell MB, Vaithiyalingam S, Nourse A, Li Z, Woetzel N, Alexander N, Meiler J, White SW Proc Natl Acad Sci U S A. 2016 Mar 22;113(12):3275-80. doi:, 10.1073/pnas.1519154113. Epub 2016 Mar 7. PMID:26951671[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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