2r9l
From Proteopedia
(New page: 200px<br /><applet load="2r9l" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r9l, resolution 2.400Å" /> '''Polymerase Domain f...) |
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==Overview== | ==Overview== | ||
| - | Nonhomologous end joining (NHEJ) is a critical DNA double-strand break | + | 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== | ==About this Structure== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Brissett, N | + | [[Category: Brissett, N C.]] |
| - | [[Category: Doherty, A | + | [[Category: Doherty, A J.]] |
| - | [[Category: Fox, G | + | [[Category: Fox, G C.]] |
| - | [[Category: Pitcher, R | + | [[Category: Pitcher, R S.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: PEG]] | [[Category: PEG]] | ||
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[[Category: transferase/dna complex]] | [[Category: transferase/dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:45:39 2008'' |
Revision as of 16:45, 21 February 2008
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Polymerase Domain from Mycobacterium tuberculosis Ligase D in complex with DNA
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 and 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 Thu Feb 21 18:45:39 2008
