Crystal Structures of the Streptomyces coelicolor TetR-Like Protein ActR Alone and in Complex with Actinorhodin or the Actinorhodin Biosynthetic Precursor (S)-DNPA

Willems, Andrew; Tahlan, Kapil; Taguchi, Tanezo; Zhang, K.; Z.Z., Lee,; Ichinose, Koji; Junop, M.S.; Nodwell, Justin R.

doi:10.1016/j.jmb.2007.12.061

Cited by 60 publications

(63 citation statements)

References 49 publications

(52 reference statements)

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“…This is also seen for the ligand-binding pockets of the majority of TFRs (e.g., ActR, CmeR, and QacR [53,54,56]). In contrast, the SimR ligand-binding cavity is composed of residues from both monomers such that each binds either the aminocoumarin or the angucyclinone moiety of the simocyclinone ligand (50).…”

Section: Tfr-ligand Interactionsmentioning

confidence: 64%

“…8). For example, ActR, QacR, SmeT, TetR, and TtgR all have a "side entry" opening distal to the dimerization interface that is believed to be the site of access for different ligands (22,(51)(52)(53)(54). Ligands appear to enter CmeR, CgmR, HrtR, LfrR, and SimR via an entry point closer to the "front" of the protein (43,46,50,55,56).…”

Section: Tfr-ligand Interactionsmentioning

confidence: 99%

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The TetR Family of Regulators

Cuthbertson

Nodwell

2013

Microbiol Mol Biol Rev

451

512

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SUMMARY The most common prokaryotic signal transduction mechanisms are the one-component systems in which a single polypeptide contains both a sensory domain and a DNA-binding domain. Among the >20 classes of one-component systems, the TetR family of regulators (TFRs) are widely associated with antibiotic resistance and the regulation of genes encoding small-molecule exporters. However, TFRs play a much broader role, controlling genes involved in metabolism, antibiotic production, quorum sensing, and many other aspects of prokaryotic physiology. There are several well-established model systems for understanding these important proteins, and structural studies have begun to unveil the mechanisms by which they bind DNA and recognize small-molecule ligands. The sequences for more than 200,000 TFRs are available in the public databases, and genomics studies are identifying their target genes. Three-dimensional structures have been solved for close to 200 TFRs. Comparison of these structures reveals a common overall architecture of nine conserved α helices. The most important open question concerning TFR biology is the nature and diversity of their ligands and how these relate to the biochemical processes under their control.

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Section: Tfr-ligand Interactionsmentioning

confidence: 64%

Section: Tfr-ligand Interactionsmentioning

confidence: 99%

The TetR Family of Regulators

Cuthbertson

Nodwell

2013

Microbiol Mol Biol Rev

451

512

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“…2) to that of T. thermophilus PaaR, among the proteins with solved three-dimensional structures. The putative T. thermophilus PaaR structure adopts the typical three-dimensional structure of the TetR family proteins (1,12,23,24,28), with 10 ␣-helices (see Fig. S2A in the supplemental material).…”

Section: Resultsmentioning

confidence: 99%

Phenylacetyl Coenzyme A Is an Effector Molecule of the TetR Family Transcriptional Repressor PaaR from Thermus thermophilusHB8

et al. 2011

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“…The distance between the two Ca atoms of the amino acid residues located in the centre of the a3 helices (Y44) of B. subtilis FadR (the DNA-binding form), which possibly interact with the major groove of DNA, is~4 Å shorter than in the case of T. thermophilus FadR (the DNA-unbound form); thus, no dramatic structural differences were found between the two structures. The transition between the DNA-bound and -unbound forms of T. thermophilus FadR might be subtle or difficult to observe, as in the case of another TetR-family protein, Streptomyces coelicolor ActR (Willems et al, 2008). Further biochemical and structural studies will be needed to elucidate the regulatory mechanism of FadR, and the fatty acid degradation system of this thermophilic bacterium.…”

Section: Discussionmentioning

confidence: 99%

TetR-family transcriptional repressor Thermus thermophilus FadR controls fatty acid degradation

Agari

Sakamoto

et al. 2011

Microbiology

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In the extremely thermophilic bacterium Thermus thermophilus HB8, one of the four TetR-family transcriptional regulators, which we named T. thermophilus FadR, negatively regulated the expression of several genes, including those involved in fatty acid degradation, both in vivo and in vitro. T. thermophilus FadR repressed the expression of the target genes by binding pseudopalindromic sequences covering the predicted "10 hexamers of their promoters, and medium-to-long straight-chain (C10-18) fatty acyl-CoA molecules were effective for transcriptional derepression. An X-ray crystal structure analysis revealed that T. thermophilus FadR bound one lauroyl (C12)-CoA molecule per FadR monomer, with its acyl chain moiety in the centre of the FadR molecule, enclosed within a tunnel-like substrate-binding pocket surrounded by hydrophobic residues, and the CoA moiety interacting with basic residues on the protein surface. The growth of T. thermophilus HB8, with palmitic acid as the sole carbon source, increased the expression of FadR-regulated genes. These results indicate that in T. thermophilus HB8, medium-to-long straight-chain fatty acids can be used for metabolic energy under the control of FadR, although the major fatty acids found in this strain are iso-and anteiso-branchedchain (C15 and 17) fatty acids.

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Crystal Structures of the Streptomyces coelicolor TetR-Like Protein ActR Alone and in Complex with Actinorhodin or the Actinorhodin Biosynthetic Precursor (S)-DNPA

Cited by 60 publications

References 49 publications

The TetR Family of Regulators

The TetR Family of Regulators

Phenylacetyl Coenzyme A Is an Effector Molecule of the TetR Family Transcriptional Repressor PaaR from Thermus thermophilusHB8

TetR-family transcriptional repressor Thermus thermophilus FadR controls fatty acid degradation

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