3C95
Exonuclease I (apo)
Summary for 3C95
Entry DOI | 10.2210/pdb3c95/pdb |
Related | 1FXX 2C94 |
Descriptor | Exodeoxyribonuclease I, MAGNESIUM ION (3 entities in total) |
Functional Keywords | exonuclease, ssb, genome maintenance, dna damage, dna repair, hydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 55534.87 |
Authors | Keck, J.L.,Lu, D. (deposition date: 2008-02-15, release date: 2008-07-08, Last modification date: 2023-08-30) |
Primary citation | Lu, D.,Keck, J.L. Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I. Proc.Natl.Acad.Sci.USA, 105:9169-9174, 2008 Cited by PubMed Abstract: Bacterial single-stranded DNA (ssDNA)-binding proteins (SSBs) play essential protective roles in genome biology by shielding ssDNA from damage and preventing spurious DNA annealing. Far from being inert, ssDNA/SSB complexes are dynamic DNA processing centers where many different enzymes gain access to genomic substrates by exploiting direct interactions with SSB. In all cases examined to date, the C terminus of SSB (SSB-Ct) forms the docking site for heterologous proteins. We describe the 2.7-A-resolution crystal structure of a complex formed between a peptide comprising the SSB-Ct element and exonuclease I (ExoI) from Escherichia coli. Two SSB-Ct peptides bind to adjacent sites on ExoI. Mutagenesis studies indicate that one of these sites is important for association with the SSB-Ct peptide in solution and for SSB stimulation of ExoI activity, whereas the second has no discernable function. These studies identify a correlation between the stability of the ExoI/SSB-Ct complex and SSB-stimulation of ExoI activity. Furthermore, mutations within SSB's C terminus produce variants that fail to stimulate ExoI activity, whereas the SSB-Ct peptide alone has no effect. Together, our findings indicate that SSB stimulates ExoI by recruiting the enzyme to its substrate and provide a structural paradigm for understanding SSB's organizational role in genome maintenance. PubMed: 18591666DOI: 10.1073/pnas.0800741105 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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