scholarly journals Crystal structure of theDNA‐binding domain of the LysR‐type transcriptional regulator CbnR in complex with aDNAfragment of the recognition‐binding site in the promoter region

FEBS Journal ◽  
2018 ◽  
Vol 285 (5) ◽  
pp. 977-989 ◽  
Author(s):  
Maharani Pertiwi Koentjoro ◽  
Naruhiko Adachi ◽  
Miki Senda ◽  
Naoto Ogawa ◽  
Toshiya Senda
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Promoter Region ◽  
Transcriptional Regulator ◽  
Binding Domain

scholarly journals Crystal Structure of the DNA-binding Domain of the LysR-type Transcriptional Regulator CbnR in Complex with a DNA Fragment of the Recognition-binding Site

2018 ◽  
Vol 60 (2-3) ◽  
pp. 135-141
Author(s):  
Miki SENDA ◽  
Naruhiko ADACHI ◽  
Toshiya SENDA ◽  
Maharani Pertiwi KOENTJORO ◽  
Naoto OGAWA
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Binding Site ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Dna Fragment

scholarly journals Crystal structure of the N-terminal domain of VqsR fromPseudomonas aeruginosaat 2.1 Å resolution

2017 ◽  
Vol 73 (7) ◽  
pp. 431-436
Author(s):  
Qing He ◽  
Kang Wang ◽  
Tiantian Su ◽  
Feng Wang ◽  
Lichuan Gu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sequence Similarity ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Structural Comparison ◽  
Homoserine Lactones ◽  
Terminal Domain ◽  
C Terminus ◽  
Common Motif ◽  
The Common

VqsR is a quorum-sensing (QS) transcriptional regulator which controls QS systems (las,rhlandpqs) by directly downregulating the expression ofqscRinPseudomonas aeruginosa. As a member of the LuxR family of proteins, VqsR shares the common motif of a helix–turn–helix (HTH)-type DNA-binding domain at the C-terminus, while the function of its N-terminal domain remains obscure. Here, the crystal structure of the N-terminal domain of VqsR (VqsR-N; residues 1–193) was determined at a resolution of 2.1 Å. The structure is folded into a regular α–β–α sandwich topology, which is similar to the ligand-binding domain (LBD) of the LuxR-type QS receptors. Although their sequence similarity is very low, structural comparison reveals that VqsR-N has a conserved enclosed cavity which could recognize acyl-homoserine lactones (AHLs) as in other LuxR-type AHL receptors. The structure suggests that VqsR could be a potential AHL receptor.

scholarly journals Crystal Structure of the Sugar Binding Domain of the Archaeal Transcriptional Regulator TrmB

2006 ◽  
Vol 281 (16) ◽  
pp. 10976-10982 ◽  
Author(s):  
Michael Krug ◽  
Sung-Jae Lee ◽  
Kay Diederichs ◽  
Winfried Boos ◽  
Wolfram Welte
Keyword(s):  
Crystal Structure ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Sugar Binding

scholarly journals Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose 1,5-bisphosphate

2018 ◽  
Vol 74 (8) ◽  
pp. 506-511 ◽  
Author(s):  
Didel M. Mahounga ◽  
Hui Sun ◽  
Yong-Liang Jiang
Keyword(s):  
Crystal Structure ◽  
Transcriptional Regulator ◽  
Synechococcus Elongatus ◽  
Binding Domain ◽  
Binding Pattern ◽  
Structural Comparison ◽  
Sequence Analyses ◽  
Dimeric Structure ◽  
Pcc 7942 ◽  
Effector Binding

The CO2-concentrating mechanism (CCM) has evolved to improve the efficiency of photosynthesis in autotrophic cyanobacteria. CmpR, a LysR-type transcriptional regulator (LTTR) from Synechococcus elongatus PCC 7942, was found to regulate CCM-related genes under low-CO2 conditions. Here, the dimeric structure of the effector-binding domain of CmpR (CmpR-EBD) in complex with the co-activator ribulose 1,5-bisphosphate (RuBP) is reported at 2.15 Å resolution. One RuBP molecule binds to the inter-domain cleft between the two subunits of the CmpR-EBD dimer. Structural comparison combined with sequence analyses demonstrated that CmpR-EBD has an overall structure similar to those of LTTRs of known structure, but possesses a distinctly different effector-binding pattern.

scholarly journals The Crystal Structure of ELIC in Complex with Chlorpromazine Unexpectedly Unveils an Allosteric Binding Site in the Ligand-Binding Domain

2016 ◽  
Vol 110 (3) ◽  
pp. 457a
Author(s):  
Mieke Nys ◽  
Ana Farinha ◽  
Eveline Wijckmans ◽  
Marijke Brams ◽  
Özge Yoluk ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Binding Site ◽  
Binding Domain ◽  
Ligand Binding Domain

scholarly journals Crystal structure of the ligand-binding domain of a LysR-type transcriptional regulator: transcriptional activation via a rotary switch

2018 ◽  
Vol 110 (4) ◽  
pp. 550-561 ◽  
Author(s):  
Youngchang Kim ◽  
Gekleng Chhor ◽  
Ching-Sung Tsai ◽  
James B. Winans ◽  
Robert Jedrzejczak ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Transcriptional Activation ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Rotary Switch
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