4lty: Difference between revisions
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==Crystal Structure of E.coli SbcD at 1.8 A Resolution== | ==Crystal Structure of E.coli SbcD at 1.8 A Resolution== | ||
<StructureSection load='4lty' size='340' side='right' caption='[[4lty]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4lty' size='340' side='right'caption='[[4lty]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lty]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4lty]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_KO11FL Escherichia coli KO11FL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LTY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4lty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lty OCA], [https://pdbe.org/4lty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lty RCSB], [https://www.ebi.ac.uk/pdbsum/4lty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lty ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Exonuclease|Exonuclease]] | *[[Exonuclease 3D structures|Exonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli KO11FL]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Liang DC]] | ||
[[Category: | [[Category: Liu S]] | ||
[[Category: | [[Category: Tian LF]] | ||
[[Category: | [[Category: Yan XX]] | ||
Revision as of 13:32, 21 December 2022
Crystal Structure of E.coli SbcD at 1.8 A ResolutionCrystal Structure of E.coli SbcD at 1.8 A Resolution
Structural highlights
Publication Abstract from PubMedThe Mre11 complex comprising meiotic recombination 11 (Mre11), Rad50 and Nijmegen breakage syndrome 1 (Nbs1) plays multiple important roles in the sensing, processing and repair of DNA double-strand breaks (DSBs). Here, crystal structures of the Escherichia coli Mre11 homologue SbcD and its Mn(2+) complex are reported. Dimerization of SbcD depends on a four-helix bundle consisting of helices alpha2, alpha3, alpha2' and alpha3' of the two monomers, and the irregular and bent conformation of helices alpha3 and alpha3' in the SbcD dimer results in a dimeric arrangement that differs from those of previously reported Mre11 dimers. This finding indicates a distinct selectivity in DNA substrate recognition. The biochemical data combined with the crystal structures revealed that the SbcD monomer exhibits single-stranded DNA (ssDNA) endonuclease activity and double-stranded DNA (dsDNA) exonuclease activity on the addition of a high concentration of Mn(2+). For the first time, atomic force microscopy analysis has been used to demonstrate that the SbcD monomer also possesses Mn(2+)-dependent dsDNA endonuclease activity. Loop beta7-alpha6 of SbcD is likely to be a molecular switch and plays an important role in the regulation of substrate binding, catalytic reaction and state transitions. Based on structural and mutational analyses, a novel ssDNA-binding model of SbcD is proposed, providing insight into the catalytic mechanism of DSBs repair by the Mre11 complex. Structural basis for DNA recognition and nuclease processing by the Mre11 homologue SbcD in double-strand breaks repair.,Liu S, Tian LF, Liu YP, An XM, Tang Q, Yan XX, Liang DC Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):299-309. doi:, 10.1107/S139900471302693X. Epub 2014 Jan 29. PMID:24531464[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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