6bhw: Difference between revisions
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<StructureSection load='6bhw' size='340' side='right'caption='[[6bhw]], [[Resolution|resolution]] 2.21Å' scene=''> | <StructureSection load='6bhw' size='340' side='right'caption='[[6bhw]], [[Resolution|resolution]] 2.21Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6bhw]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6bhw]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BHW FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.208Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=6bhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bhw OCA], [https://pdbe.org/6bhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bhw RCSB], [https://www.ebi.ac.uk/pdbsum/6bhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bhw ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SSBA_BACSU SSBA_BACSU] 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 (PubMed:21170359). Has a 20-fold higher affinity for ssDNA than SsbB; SsbA and DprA activate the homologuos DNA strand exchange function of RecA-ATP (PubMed:25138221).<ref>PMID:25138221</ref> <ref>PMID:21170359</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6bhw" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6bhw" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dubiel | [[Category: Dubiel KD]] | ||
[[Category: Keck | [[Category: Keck JL]] | ||
[[Category: Myers | [[Category: Myers AR]] | ||
[[Category: Satyshur | [[Category: Satyshur KA]] | ||
Latest revision as of 17:41, 4 October 2023
B. subtilis SsbAB. subtilis SsbA
Structural highlights
FunctionSSBA_BACSU 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 (PubMed:21170359). Has a 20-fold higher affinity for ssDNA than SsbB; SsbA and DprA activate the homologuos DNA strand exchange function of RecA-ATP (PubMed:25138221).[1] [2] Publication Abstract from PubMedBacteria encode homooligomeric single-stranded (ss) DNA-binding proteins (SSBs) that coat and protect ssDNA intermediates formed during genome maintenance reactions. The prototypical Escherichia coli SSB tetramer can bind ssDNA using multiple modes that differ by the number of bases bound per tetramer and the magnitude of the binding cooperativity. Our understanding of the mechanisms underlying cooperative ssDNA binding by SSBs has been hampered by the limited amount of structural information available for interfaces that link adjacent SSB proteins on ssDNA. Here we present a crystal structure of Bacillus subtilis SsbA bound to ssDNA. The structure resolves SsbA tetramers joined together by a ssDNA "bridge" and identifies an interface, termed the "bridge interface," that links adjacent SSB tetramers through an evolutionarily conserved surface near the ssDNA-binding site. E. coli SSB variants with altered bridge interface residues bind ssDNA with reduced cooperativity and with an altered distribution of DNA binding modes. These variants are also more readily displaced from ssDNA by RecA than wild-type SSB. In spite of these biochemical differences, each variant is able to complement deletion of the ssb gene in E. coli. Together our data suggest a model in which the bridge interface contributes to cooperative ssDNA binding and SSB function but that destabilization of the bridge interface is tolerated in cells. Structural Mechanisms of Cooperative DNA Binding by Bacterial Single-Stranded DNA-Binding Proteins.,Dubiel K, Myers AR, Kozlov AG, Yang O, Zhang J, Ha T, Lohman TM, Keck JL J Mol Biol. 2018 Nov 22. pii: S0022-2836(18)31046-5. doi:, 10.1016/j.jmb.2018.11.019. PMID:30472092[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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