Transcription Factor

Accessions: 3clc_A (3D-footprint 20231221), 3clc_D (3D-footprint 20231221), 3s8q_A (3D-footprint 20231221), 3ufd_A (3D-footprint 20231221), 3ufd_E (3D-footprint 20231221), 4iwr_B (3D-footprint 20231221), 4iwr_F (3D-footprint 20231221), 4x4b_A (3D-footprint 20231221), 4x4b_D (3D-footprint 20231221), 4x4c_A (3D-footprint 20231221), 4x4c_D (3D-footprint 20231221), 4x4d_A (3D-footprint 20231221), 4x4d_D (3D-footprint 20231221), 4x4e_A (3D-footprint 20231221), 4x4e_D (3D-footprint 20231221), 4x4f_A (3D-footprint 20231221), 4x4f_D (3D-footprint 20231221), 4x4g_A (3D-footprint 20231221), 4x4g_D (3D-footprint 20231221), 4x4h_A (3D-footprint 20231221), 4x4h_D (3D-footprint 20231221), 4x4i_A (3D-footprint 20231221), 4x4i_D (3D-footprint 20231221)
Names: Q8GGH0_9ENTR, Regulatory protein, R-M CONTROLLER PROTEIN
Organisms: Enterobacter sp. RFL1396
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]
Uniprot: Q8GGH0
Length: 76
Pfam Domains: 12-62 Helix-turn-helix
12-62 Helix-turn-helix domain
Sequence:
(in bold interface residues)
1 ESFLLSKVSFVIKKIRLEKGMTQEDLAYKSNLDRTYISGIERNSRNLTIKSLELIMKGLE 60
61 VSDVVFFEMLIKEILK
Interface Residues: 24, 33, 34, 35, 36, 38, 39, 42, 44, 45
3D-footprint Homologues: 3zkc_A, 8ity_P, 3s8q_A, 3u3w_B
Binding Motifs: 3clc_ABCD TGTnGACnnnnGnCACACGGnCnnnnATTCACA
3s8q_A TGTGACnta
3s8q_AB TGTGACnTAtAGTCCG
3ufd_AB TGTCGACTATAGTCTACA
3ufd_E TGTAGAC
4iwr_AB TGTGACnnnnnnTCcG
4iwr_EF CGGAmnnnnnGTCACA
4iwr_F gTCcG
4x4b_ABCD TGTnGAcnnnnTnCACrCnGannnnnAGTcACA
4x4c_ABCD TGTGACTnnnnnTCnGCGTGnAnnnnGTCnACA
4x4d_ABCD TGTGACTnnnnntCnGyGTGnAnnnngTCnACA
4x4e_ABCD TGTnGACnnnnTnCACRCnGannnnnAGTcACA
4x4f_ABCD TGTGACTnnnnntCnGyGTGnAnnnnGTCnACA
4x4g_ABCD TGTnGACnnnnTnCACRCnGAnnnnnAGTCACA
4x4h_ABCD TGTGACTnnnnntCnGyGTGnAnnnngTCnACA
4x4i_ABCD TGTGACTnnnnnTCnGYGTGnAnnnnGTCnACA
Binding Sites: 3clc_E / 4x4b_E / 4x4c_E / 4x4d_E / 4x4e_E / 4x4f_E / 4x4g_E / 4x4h_E / 4x4i_E
3clc_F / 4x4b_F / 4x4c_F / 4x4d_F / 4x4e_F / 4x4f_F / 4x4g_F / 4x4h_F / 4x4i_F
3s8q_C
3s8q_D
3ufd_G
3ufd_H
4iwr_C
4iwr_D
4iwr_G
4iwr_H
Publications: McGeehan J.E, Streeter S.D, Thresh S.J, Ball N, Ravelli R.B, Kneale G.G. Structural analysis of the genetic switch that regulates the expression of restriction-modification genes. Nucleic acids research 36:4778-87 (2008). [Pubmed]

McGeehan J.E, Ball N.J, Streeter S.D, Thresh S.J, Kneale G.G. Recognition of dual symmetry by the controller protein C.Esp1396I based on the structure of the transcriptional activation complex. Nucleic acids research 40:4158-67 (2012). [Pubmed]

Ball N.J, McGeehan J.E, Streeter S.D, Thresh S.J, Kneale G.G. The structural basis of differential DNA sequence recognition by restriction-modification controller proteins. Nucleic acids research 40:10532-42 (2012). [Pubmed]

Martin RN, McGeehan JE, Ball NJ, Streeter SD, Thresh SJ, Kneale GG. Structural analysis of DNA-protein complexes regulating the restriction-modification system Esp1396I. Acta Crystallogr Sect F Struct Biol Cryst Commun : (2013). [Pubmed]

Bury C, Garman EF, Ginn HM, Ravelli RB, Carmichael I, Kneale G, McGeehan JE. Radiation damage to nucleoprotein complexes in macromolecular crystallography. J Synchrotron Radiat 22:213-24 (2015). [Pubmed]
Related annotations: PaperBLAST

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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.