2NMV
Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA
Summary for 2NMV
Entry DOI | 10.2210/pdb2nmv/pdb |
Related | 2D7D |
Descriptor | 5'-D(P*TP*TP*TP*TP*T)-3', UvrABC system protein B, N-METHYLACETAMIDE, ... (6 entities in total) |
Functional Keywords | protein-dna complex, t-fluorescein, hairpin, hydrolase-dna complex, hydrolase/dna |
Biological source | Bacillus subtilis More |
Cellular location | Cytoplasm (By similarity): P37954 P37954 |
Total number of polymer chains | 3 |
Total formula weight | 83254.97 |
Authors | Waters, T.R.,Eryilmaz, J.,Geddes, S.,Barrett, T.E. (deposition date: 2006-10-23, release date: 2007-01-16, Last modification date: 2023-10-25) |
Primary citation | Waters, T.R.,Eryilmaz, J.,Geddes, S.,Barrett, T.E. Damage detection by the UvrABC pathway: crystal structure of UvrB bound to fluorescein-adducted DNA Febs Lett., 580:6423-6427, 2006 Cited by PubMed Abstract: UvrB is the damage recognition element of the highly conserved UvrABC pathway that functions in the removal of bulky DNA adducts. Pivotal to this is the formation of a damage detection complex that relies on the ability of UvrB to locate and sequester diverse lesions. Whilst structures of UvrB bound to DNA have recently been reported, none address the issue of lesion recognition. Here, we describe the crystal structure of UvrB bound to a pentanucleotide containing a single fluorescein-adducted thymine that reveals a unique mechanism for damage detection entirely dependent on the exclusion of lesions larger than an undamaged nucleotide. PubMed: 17097086DOI: 10.1016/j.febslet.2006.10.051 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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