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3C95

Exonuclease I (apo)

Summary for 3C95
Entry DOI10.2210/pdb3c95/pdb
Related1FXX 2C94
DescriptorExodeoxyribonuclease I, MAGNESIUM ION (3 entities in total)
Functional Keywordsexonuclease, ssb, genome maintenance, dna damage, dna repair, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight55534.87
Authors
Keck, J.L.,Lu, D. (deposition date: 2008-02-15, release date: 2008-07-08, Last modification date: 2023-08-30)
Primary citationLu, 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: 18591666
DOI: 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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