Ribbon diagram of dimeric structure of BtAraR. The N-te

A novel transcriptional regulator of L-arabinose utilization in human gut bacteria. Chang C, Tesar C, Li X, Kim Y, Rodionov DA, Joachimiak A - Nucleic Acids Res. (2015) Bottom Line: L-arabinose was confirmed to be a negative effector of BtAraR.In the structure of the BtAraR-DNA complex, we found the unique interaction of arginine intercalating its guanidinum moiety into the base pair stacking of B-DNA.L-arabinose binding induces movement of wHTH domains, resulting in a conformation unsuitable for DNA binding. View Article: PubMed Central - PubMed Affiliation: Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL 60439, USA Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, IL 60439, USA. Show MeSH Major Arabinose/chemistry/metabolism* Bacterial Proteins/chemistry/metabolism Bacteroides/genetics Transcription Factors/chemistry/metabolism Minor* Arginine/chemistry Binding Sites DNA, Bacterial/chemistry/metabolism Humans Models, Molecular Operator Regions, Genetic Protein Binding Protein Structure, Tertiary Regulon	© Copyright Policy - creative-commons Related In: Results - Collection License Show All Figures getmorefigures.php?uid=PMC4666351&req=5 Figure 3: Ribbon diagram of dimeric structure of BtAraR. The N-terminal domain is colored as cyan, the C-terminal domain is colored as green. Molecule B is represented as paled color. The secondary structures are labeled. Mentions: The overall structure of BtAraR is quite similar to the previously solved NrtR protein (29% sequence identity), an ADP-ribose-dependent transcriptional regulator from S. oneidensis (17). The biological unit appears to be a dimer while a monomer is composed of two domains. The N-terminal domain (residues 1–148, Nudix domain) shows a Nudix hydrolase fold containing three α-helices and a seven-stranded β sheet along with an extra N-terminal helix of less than a turn. The C-terminal domain (residues 149–225) is a winged helix-turn-helix (wHTH) DNA-binding domain that has a protruding β-hairpin as a wing, and it is predicted to bind the major groove surface of the DNA using the HTH motif and the minor groove surface using the wing (Figure 3; Supplementary Figures S1 and S2).

A novel transcriptional regulator of L-arabinose utilization in human gut bacteria.

Chang C, Tesar C, Li X, Kim Y, Rodionov DA, Joachimiak A - Nucleic Acids Res. (2015)

Bottom Line: L-arabinose was confirmed to be a negative effector of BtAraR.In the structure of the BtAraR-DNA complex, we found the unique interaction of arginine intercalating its guanidinum moiety into the base pair stacking of B-DNA.L-arabinose binding induces movement of wHTH domains, resulting in a conformation unsuitable for DNA binding.

View Article: PubMed Central - PubMed

Affiliation: Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL 60439, USA Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, IL 60439, USA.

Show MeSH

Ribbon diagram of dimeric structure of BtAraR. The N-terminal domain is colored as cyan, the C-terminal domain is colored as green. Molecule B is represented as paled color. The secondary structures are labeled.

Related In: Results - Collection

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Figure 3: Ribbon diagram of dimeric structure of BtAraR. The N-terminal domain is colored as cyan, the C-terminal domain is colored as green. Molecule B is represented as paled color. The secondary structures are labeled.

Mentions: The overall structure of BtAraR is quite similar to the previously solved NrtR protein (29% sequence identity), an ADP-ribose-dependent transcriptional regulator from S. oneidensis (17). The biological unit appears to be a dimer while a monomer is composed of two domains. The N-terminal domain (residues 1–148, Nudix domain) shows a Nudix hydrolase fold containing three α-helices and a seven-stranded β sheet along with an extra N-terminal helix of less than a turn. The C-terminal domain (residues 149–225) is a winged helix-turn-helix (wHTH) DNA-binding domain that has a protruding β-hairpin as a wing, and it is predicted to bind the major groove surface of the DNA using the HTH motif and the minor groove surface using the wing (Figure 3; Supplementary Figures S1 and S2).