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Title: The crystal structure of the effector-binding domain of the trehalose repressor TreR from Bacillus subtilis 168 reveals a unigue quarternary assembly.

Abstract

No abstract prepared.

Authors:
; ; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
928947
Report Number(s):
ANL/BIO/JA-61338
TRN: US200811%%438
DOE Contract Number:
DE-AC02-06CH11357
Resource Type:
Journal Article
Resource Relation:
Journal Name: Proteins: Struct. Function Bioinform.; Journal Volume: 69; Journal Issue: 3 ; 2007
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; BACILLUS SUBTILIS; CRYSTAL STRUCTURE; ANL

Citation Formats

Rezacova, P., Krejcirikova, V., Borek, D, Moy, S, Joachimiak, A, Otwinowski, Z, Biosciences Division, and Univ. of Texas Southwestern Medical Center at Dallas. The crystal structure of the effector-binding domain of the trehalose repressor TreR from Bacillus subtilis 168 reveals a unigue quarternary assembly.. United States: N. p., 2007. Web. doi:10.1002/prot.21516.
Rezacova, P., Krejcirikova, V., Borek, D, Moy, S, Joachimiak, A, Otwinowski, Z, Biosciences Division, & Univ. of Texas Southwestern Medical Center at Dallas. The crystal structure of the effector-binding domain of the trehalose repressor TreR from Bacillus subtilis 168 reveals a unigue quarternary assembly.. United States. doi:10.1002/prot.21516.
Rezacova, P., Krejcirikova, V., Borek, D, Moy, S, Joachimiak, A, Otwinowski, Z, Biosciences Division, and Univ. of Texas Southwestern Medical Center at Dallas. Mon . "The crystal structure of the effector-binding domain of the trehalose repressor TreR from Bacillus subtilis 168 reveals a unigue quarternary assembly.". United States. doi:10.1002/prot.21516.
@article{osti_928947,
title = {The crystal structure of the effector-binding domain of the trehalose repressor TreR from Bacillus subtilis 168 reveals a unigue quarternary assembly.},
author = {Rezacova, P. and Krejcirikova, V. and Borek, D and Moy, S and Joachimiak, A and Otwinowski, Z and Biosciences Division and Univ. of Texas Southwestern Medical Center at Dallas},
abstractNote = {No abstract prepared.},
doi = {10.1002/prot.21516},
journal = {Proteins: Struct. Function Bioinform.},
number = 3 ; 2007,
volume = 69,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}
  • The crystal structure of the effector-binding domain of the transcriptional repressor AraR from B. subtilis in complex with the effector molecule (l-arabinose) was determined at 2.2 Å resolution. A detailed analysis of the crystal identified a dimer organization that is distinctive from that of other members of the GalR/LacI family. In Bacillus subtilis, the arabinose repressor AraR negatively controls the expression of genes in the metabolic pathway of arabinose-containing polysaccharides. The protein is composed of two domains of different phylogenetic origin and function: an N-terminal DNA-binding domain belonging to the GntR family and a C-terminal effector-binding domain that shows similaritymore » to members of the GalR/LacI family. The crystal structure of the C-terminal effector-binding domain of AraR in complex with the effector l-arabinose has been determined at 2.2 Å resolution. The l-arabinose binding affinity was characterized by isothermal titration calorimetry and differential scanning fluorimetry; the K{sub d} value was 8.4 ± 0.4 µM. The effect of l-arabinose on the protein oligomeric state was investigated in solution and detailed analysis of the crystal identified a dimer organization which is distinctive from that of other members of the GalR/LacI family.« less
  • The structure of the winged helix–turn–helix DNA-binding domain of AhrC has been determined at 1.0 Å resolution. The largely hydrophobic β-wing shows high B factors and may mediate the dimer interface in operator complexes. In Bacillus subtilis the concentration of l-arginine is controlled by the transcriptional regulator AhrC, which interacts with 18 bp DNA operator sites called ARG boxes in the promoters of arginine biosynthetic and catabolic operons. AhrC is a 100 kDa homohexamer, with each subunit having two domains. The C-terminal domains form the core, mediating intersubunit interactions and binding of the co-repressor l-arginine, whilst the N-terminal domains containmore » a winged helix–turn–helix DNA-binding motif and are arranged around the periphery. The N-terminal domain of AhrC has been expressed, purified and characterized and it has been shown that the fragment still binds DNA operators as a recombinant monomer. The DNA-binding domain has also been crystallized and the crystal structure refined to 1.0 Å resolution is presented.« less
  • No abstract prepared.
  • The Bacillus subtilis Spx protein is a global transcription factor that interacts with the C-terminal domain of the RNA polymerase {alpha} subunit ({alpha}CTD) and regulates transcription of genes involved in thiol-oxidative stress, sporulation, competence, and organosulfur metabolism. Here we determined the X-ray crystal structure of the Spx/{alpha}CTD complex from an entirely new crystal form than previously reported [Newberry, K.J., Nakano, S., Zuber, P., Brennan, R.G., 2005. Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. Proc. Natl. Acad. Sci. USA 102, 15839-15844]. Comparison of the previously reported sulfate-boundmore » complex and our sulfate-free complex reveals subtle conformational changes that may be important for the role of Spx in regulating organosulfur metabolism.« less