DNA Binding Site

Accessions: 1bdh_B (3D-footprint 20231221), 1bdi_B (3D-footprint 20231221), 1jfs_B (3D-footprint 20231221), 1jft_B (3D-footprint 20231221), 1qpz_M (3D-footprint 20231221), 1vpw_B (3D-footprint 20231221), 2pua_B (3D-footprint 20231221), 2pub_B (3D-footprint 20231221), 2puc_B (3D-footprint 20231221), 2pud_B (3D-footprint 20231221), 2pue_B (3D-footprint 20231221), 2puf_B (3D-footprint 20231221), 2pug_B (3D-footprint 20231221)
Organisms: Escherichia coli, strain K12
Libraries: 3D-footprint 20231221 1
1 Contreras-Moreira B. 3D-footprint: a database for the structural analysis of protein-DNA complexes. Nucleic acids research 38:D91-7 (2010). [Pubmed]
Length: 17
Sequence: TACGCAAACGTTTGCGT
Type: Heterodimer
Binding TFs: 1bdh_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
1bdi_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
1jfs_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
1jft_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
1vpw_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
2pua_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
2pub_A / 2puc_A / 2pud_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
2pue_A / 2puf_A / 2pug_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
1qpz_A (Bacterial regulatory proteins, lacI family, Periplasmic binding proteins and sugar binding domain of LacI family, Periplasmic binding protein-like domain, Periplasmic binding protein domain)
Binding Motifs: 1jfs_A CGcanACg
1vpw_A CGCanACG
2pub_A CGcanACg
2puc_A CGcanACg
2pug_A CGcanACg
1qpz_A CGcanACg
2pua_A CGCanACg
2pue_A CGCanACg
2pud_A CGcnnACg
2puf_A CGCanACg
1bdh_A CGcnnnCg
1bdi_A CGCanACg
1jft_A CGCnnACG
Publications: Huffman J.L, Lu F, Zalkin H, Brennan R.G. Role of residue 147 in the gene regulatory function of the Escherichia coli purine repressor. Biochemistry 41:511-20 (2002). [Pubmed]

Glasfeld A, Koehler A.N, Schumacher M.A, Brennan R.G. The role of lysine 55 in determining the specificity of the purine repressor for its operators through minor groove interactions. Journal of molecular biology 291:347-61 (1999). [Pubmed]

Arvidson D.N, Lu F, Faber C, Zalkin H, Brennan R.G. The structure of PurR mutant L54M shows an alternative route to DNA kinking. Nature structural biology 5:436-41 (1998). [Pubmed]

Schumacher M.A, Choi K.Y, Zalkin H, Brennan R.G. Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices. Science (New York, N.Y.) 266:763-70 (1994). [Pubmed]

Lu F, Schumacher M.A, Arvidson D.N, Haldimann A, Wanner B.L, Zalkin H, Brennan R.G. Structure-based redesign of corepressor specificity of the Escherichia coli purine repressor by substitution of residue 190. Biochemistry 37:971-82 (1998). [Pubmed]

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These data are available AS IS and at your own risk. The EEAD/CSIC do not give any representation or warranty nor assume any liability or responsibility for the data nor the results posted (whether as to their accuracy, completeness, quality or otherwise). Access to these data is available free of charge for ordinary use in the course of research. Downloaded data have CC-BY-NC-SA license. FootprintDB is also available at RSAT::Plants, part of the INB/ELIXIR-ES resources portfolio.