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 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 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 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 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

Letter to Editor: Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional regulator with a dimeric β-barrel fold

2004 ◽  
Vol 30 (2) ◽  
pp. 211-214 ◽  
Author(s):  
Alejandro D. Nadra ◽  
Tommaso Eliseo ◽  
Yu-Keung Mok ◽  
Fabio C.L. Almeida ◽  
Mark Bycroft ◽  
...  
Keyword(s):  
Dna Binding ◽  
Solution Structure ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Hpv 16

Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure

2001 ◽  
Vol 79 (8) ◽  
pp. 692-704 ◽  
Author(s):  
Focco van den Akker
Keyword(s):  
Crystal Structure ◽  
Atrial Natriuretic Factor ◽  
Binding Protein ◽  
Chloride Ion ◽  
Binding Domain ◽  
Protein Fold ◽  
Hormone Binding ◽  
Periplasmic Binding Protein ◽  
Natriuretic Factor ◽  
Hormone Binding Domain

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

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