scholarly journals Crystal structure of the effector-binding domain of the trehalose-repressor ofescherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose

1998 ◽  
Vol 7 (12) ◽  
pp. 2511-2521 ◽  
Author(s):  
Ulrike Hars ◽  
Reinhold Horlacher ◽  
Winfried Boos ◽  
Wolfram Welte ◽  
Kay Diederichs
Keyword(s):  
Crystal Structure ◽  
Binding Domain ◽  
Ofescherichia Coli ◽  
Effector Binding ◽  
Laci Family

scholarly journals The crystal structure of the effector-binding domain of the trehalose repressor TreR from Bacillus subtilis 168 reveals a unique quarternary assembly

2007 ◽  
Vol 69 (3) ◽  
pp. 679-682 ◽  
Author(s):  
Pavlína Řezáčová ◽  
Veronika Krejčiříková ◽  
Dominika Borek ◽  
Shiu F. Moy ◽  
Andrzej Joachimiak ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Binding Domain ◽  
Bacillus Subtilis 168 ◽  
Effector 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.

Crystal Structure of the AmpR Effector Binding Domain Provides Insight into the Molecular Regulation of Inducible AmpC β-Lactamase

2010 ◽  
Vol 400 (5) ◽  
pp. 998-1010 ◽  
Author(s):  
Misty D. Balcewich ◽  
Thomas M. Reeve ◽  
Evan A. Orlikow ◽  
Lynda J. Donald ◽  
David J. Vocadlo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Domain ◽  
Molecular Regulation ◽  
Insight Into ◽  
Effector Binding

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.

Deciphering the enigma of missing DNA binding domain of LacI family transcription factors

2021 ◽  
Vol 713 ◽  
pp. 109060
Author(s):  
Neetu Neetu ◽  
Madhusudhanarao Katiki ◽  
Jai Krishna Mahto ◽  
Monica Sharma ◽  
Anoop Narayanan ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Laci Family

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.

An enzyme captured in two conformational states: crystal structure ofS-adenosyl-L-homocysteine hydrolase fromBradyrhizobium elkanii

2015 ◽  
Vol 71 (12) ◽  
pp. 2422-2432 ◽  
Author(s):  
Tomasz Manszewski ◽  
Kriti Singh ◽  
Barbara Imiolczyk ◽  
Mariusz Jaskolski
Keyword(s):  
Crystal Structure ◽  
Enzymatic Reaction ◽  
Binding Domain ◽  
Dimerization Domain ◽  
Biologically Relevant ◽  
Cofactor Binding ◽  
Enzymatic Regulation ◽  
Ligand Free ◽  
Substrate Binding Domain ◽  
Methyl Group Transfer

S-Adenosyl-L-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation ofS-adenosyl-L-methionine (SAM)-dependent methylation reactions. After methyl-group transfer from SAM,S-adenosyl-L-homocysteine (SAH) is formed as a byproduct, which in turn is hydrolyzed to adenosine (Ado) and homocysteine (Hcy) by SAHase. The crystal structure of BeSAHase, an SAHase fromBradyrhizobium elkanii, which is a nitrogen-fixing bacterial symbiont of legume plants, was determined at 1.7 Å resolution, showing the domain organization (substrate-binding domain, NAD+cofactor-binding domain and dimerization domain) of the subunits. The protein crystallized in its biologically relevant tetrameric form, with three subunits in a closed conformation enforced by complex formation with the Ado product of the enzymatic reaction. The fourth subunit is ligand-free and has an open conformation. The BeSAHase structure therefore provides a unique snapshot of the domain movement of the enzyme induced by the binding of its natural ligands.

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