5JJV

Crystal structure of XerH site-specific recombinase bound to palindromic difH substrate: post-cleavage complex

Summary for 5JJV

• Entry DOI: 10.2210/pdb5jjv/pdb
• Descriptor: Tyrosine recombinase XerH, DNA (5'-D(*TP*AP*GP*TP*TP*AP*TP*GP*AP*AP*AP*AP*C)-3'), DNA (5'-D(*TP*GP*CP*AP*GP*TP*TP*TP*TP*CP*AP*TP*AP*AP*CP*TP*A)-3'), ... (6 entities in total)
• Functional Keywords: xer, tyrosine recombinase, site-specific recombinase, chromosome dimer resolution, cell cycle, recombination
• Biological source: Helicobacter pylori (strain ATCC 700392 / 26695); More
• Total number of polymer chains: 6
• Total formula weight: 103215.42

Authors

Bebel, A.,Barabas, O. (deposition date: 2016-04-25, release date: 2016-12-28, Last modification date: 2024-10-16)

Primary citation

Bebel, A.,Karaca, E.,Kumar, B.,Stark, W.M.,Barabas, O.
Structural snapshots of Xer recombination reveal activation by synaptic complex remodeling and DNA bending.
Elife, 5:-, 2016

PubMed Abstract: Bacterial Xer site-specific recombinases play an essential genome maintenance role by unlinking chromosome multimers, but their mechanism of action has remained structurally uncharacterized. Here, we present two high-resolution structures of XerH with its recombination site DNA , representing pre-cleavage and post-cleavage synaptic intermediates in the recombination pathway. The structures reveal that activation of DNA strand cleavage and rejoining involves large conformational changes and DNA bending, suggesting how interaction with the cell division protein FtsK may license recombination at the septum. Together with biochemical and in vivo analysis, our structures also reveal how a small sequence asymmetry in defines protein conformation in the synaptic complex and orchestrates the order of DNA strand exchanges. Our results provide insights into the catalytic mechanism of Xer recombination and a model for regulation of recombination activity during cell division.

PubMed: 28009253
DOI: 10.7554/eLife.19706

Experimental method

X-RAY DIFFRACTION (2.4 Å)