scholarly journals Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.

1992 ◽  
Vol 89 (19) ◽  
pp. 9257-9261 ◽  
Author(s):  
K. P. Wilson ◽  
L. M. Shewchuk ◽  
R. G. Brennan ◽  
A. J. Otsuka ◽  
B. W. Matthews
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Dna Binding ◽  
Dna Binding Domains ◽  
Binding Domains

scholarly journals Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer

2009 ◽  
Vol 37 (6) ◽  
pp. 1962-1972 ◽  
Author(s):  
Koen Wagner ◽  
Geri Moolenaar ◽  
John van Noort ◽  
Nora Goosen
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Single Molecule ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Single Molecule Analysis

scholarly journals Structural insight into the specificity of the B3 DNA-binding domains provided by the co-crystal structure of the C-terminal fragment of BfiI restriction enzyme

2014 ◽  
Vol 42 (6) ◽  
pp. 4113-4122 ◽  
Author(s):  
Dmitrij Golovenko ◽  
Elena Manakova ◽  
Linas Zakrys ◽  
Mindaugas Zaremba ◽  
Giedrius Sasnauskas ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Restriction Enzyme ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Terminal Fragment ◽  
Structural Insight ◽  
Insight Into

scholarly journals Crystal structure of an inactive variant of the quorum-sensing master regulator HapR from the protease-deficient non-O1, non-O139Vibrio choleraestrain V2

2018 ◽  
Vol 74 (6) ◽  
pp. 331-336 ◽  
Author(s):  
Justin Cruite ◽  
Patrick Succo ◽  
Saumya Raychaudhuri ◽  
F. Jon Kull
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Quorum Sensing ◽  
Structural Alignment ◽  
Wild Type ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Phosphate Backbone ◽  
Protease Deficient ◽  
El Tor

HapR is a TetR-family transcriptional regulator that controls quorum sensing inVibrio cholerae, the causative agent of cholera. HapR regulates the expression of hemagglutinin protease, virulence and biofilm genes. The crystal structure of wild-type HapR fromV. choleraestrain O1 El Tor C6706 has previously been solved. In this study, the structure of a DNA-binding-deficient variant of HapR (HapRV2) derived from the protease-deficientV. choleraeserotype O37 strain V2 is reported. The structure reveals no structural differences compared with wild-type HapR. However, structural alignment of HapRV2with the TetR-family member QacR in complex with its operator DNA suggests that the aspartate residue located between the regulatory and DNA-binding domains may clash with and electrostatically repel the phosphate backbone of DNA to prevent binding.

scholarly journals Mechanistic Heterogeneity in Site Recognition by the Structurally Homologous DNA-binding Domains of the ETS Family Transcription Factors Ets-1 and PU.1

2014 ◽  
Vol 289 (31) ◽  
pp. 21605-21616 ◽  
Author(s):  
Shuo Wang ◽  
Miles H. Linde ◽  
Manoj Munde ◽  
Victor D. Carvalho ◽  
W. David Wilson ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Ets Family ◽  
Site Recognition

scholarly journals Protein Kinase A Signaling Pathway Regulates Transcriptional Activity of SAF-1 by Unmasking Its DNA-binding Domains

2003 ◽  
Vol 278 (25) ◽  
pp. 22586-22595 ◽  
Author(s):  
Alpana Ray ◽  
Papiya Ray ◽  
Nicole Guthrie ◽  
Arvind Shakya ◽  
Deepak Kumar ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Protein Kinase A ◽  
Signaling Pathway ◽  
Transcriptional Activity ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Kinase A
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