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Literature summary for 3.1.11.1 extracted from

  • Lu, D.; Keck, J.L.
    Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I (2008), Proc. Natl. Acad. Sci. USA, 105, 9169-9174.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.11.1

Activating Compound

Activating Compound Comment Organism Structure
additional information ssDNA-binding protein stimulates ExoI by recruiting the enzyme. ExoI/ssDNA-binding protein complex formation is necessary, but not sufficient for ssDNA-binding protein stimulation of ExoI activity Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
by hanging-drop vapor-diffusion method, unbound ExoI, to 1.7 resolution. ExoI bound to the C terminus of ssDNA-binding protein, at 2.7 A resolution. Two C terminus ssDNA-binding proteins bind to adjacent sites on ExoI Escherichia coli

Protein Variants

Protein Variants Comment Organism
D319A does not alter the secondary structure significantly. 2-fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
E150A does not alter the secondary structure significantly. 2fold enhanced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
E318A does not alter the secondary structure significantly. 2fold enhanced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
K227A does not alter the secondary structure significantly. Displays a 3fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
L331A does not alter the secondary structure significantly. Reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
Q311A does not alter the secondary structure significantly. Displays modest 2fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
R148A does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
R316A does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
R327A does not alter the secondary structure significantly. Reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
R338A does not alter the secondary structure significantly. Displays a 3fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli
Y207A does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Arg-316 rotamer position allows a nonactive site Mg2+ ion to bind to an acidic pocket formed by Glu-150, Glu-318, and Asp-319 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli ssDNA-binding protein stimulates ExoI by recruiting the enzyme to its substrate and provides a structural paradigm for understanding ssDNA-binding protein's organizational role in genome maintenance ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P04995
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ssDNA-binding protein stimulates ExoI by recruiting the enzyme to its substrate and provides a structural paradigm for understanding ssDNA-binding protein's organizational role in genome maintenance Escherichia coli ?
-
 ?
ssDNA + H2O
-
 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
ExoI
-
 Escherichia coli
exonuclease I
-
 Escherichia coli