2r9l | pdb_00002r9l
Polymerase Domain from Mycobacterium tuberculosis Ligase D in complex with DNA
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Overview
Nonhomologous end joining (NHEJ) is a critical DNA double-strand break, (DSB) repair pathway required to maintain genome stability. Many, prokaryotes possess a minimalist NHEJ apparatus required to repair DSBs, during stationary phase, composed of two conserved core proteins, Ku and, ligase D (LigD). The crystal structure of Mycobacterium tuberculosis, polymerase domain of LigD mediating the synapsis of two noncomplementary, DNA ends revealed a variety of interactions, including microhomology base, pairing, mismatched and flipped-out bases, and 3' termini forming, hairpin-like ends. Biochemical and biophysical studies confirmed that, polymerase-induced end synapsis also occurs in solution. We propose that, this DNA synaptic structure reflects an intermediate bridging stage of the, NHEJ process, before end processing and ligation, with both the polymerase, and the DNA sequence playing pivotal roles in determining the sequential, order of synapsis and remodeling before end joining.
About this Structure
2R9L is a Protein complex structure of sequences from Mycobacterium tuberculosis with EDO and PEG as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a NHEJ polymerase-mediated DNA synaptic complex., Brissett NC, Pitcher RS, Juarez R, Picher AJ, Green AJ, Dafforn TR, Fox GC, Blanco L, Doherty AJ, Science. 2007 Oct 19;318(5849):456-9. PMID:17947582
Page seeded by OCA on Wed Jan 23 11:15:52 2008
