ArticleThe EMBO journal2001
Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52 citing papers in PubMed, 149 citations in OpenAlex.
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- Improving the production of carbamoyltobramycin by an industrial Streptoalloteichus tenebrarius through metabolic engineering.Applied microbiology and biotechnology · 2024Article
- Evolution and diversification of the ACT-like domain associated with plant basic helix-loop-helix transcription factors.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Comprehensive Bioinformatics Analysis of the Biodiversity of Lsm Proteins in theMicroorganisms · 2023Article
- The Lrp/AsnC-Type Regulator PA2577 Controls the EamA-like Transporter GeneInternational journal of molecular sciences · 2021Article
- Analysis ofGenes · 2021Article
- Essentiality of the glnA gene in Haloferax mediterranei: gene conversion and transcriptional analysis.Extremophiles : life under extreme conditions · 2020Article
- CopR, a Global Regulator of Transcription to Maintain Copper Homeostasis inFrontiers in microbiology · 2020Article
- Regulation of γ-Aminobutyrate (GABA) Utilization inFrontiers in microbiology · 2020Article
- Effects of Increased 1-Aminocyclopropane-1-Carboxylate (ACC) Deaminase Activity in Bradyrhizobium sp. SUTN9-2 on Mung Bean Symbiosis under Water Deficit Conditions.Microbes and environments · 2020Article
- Alanine dehydrogenases in mycobacteria.Journal of microbiology (Seoul, Korea) · 2019Review
- Two membrane-bound transcription factors regulate expression of various type-IV-pili surface structures inPeerJ · 2019Article
- Signaling interplay between primary cilia and nitric oxide: A mini review.Nitric oxide : biology and chemistry · 2018Review
- Dissecting the Repertoire of DNA-Binding Transcription Factors of the Archaeon Pyrococcus furiosus DSM 3638.Life (Basel, Switzerland) · 2018Article
- Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-β-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains.Extremophiles : life under extreme conditions · 2016Article
- Regulation Mechanism of the ald Gene Encoding Alanine Dehydrogenase in Mycobacterium smegmatis and Mycobacterium tuberculosis by the Lrp/AsnC Family Regulator AldR.Journal of bacteriology · 2015Article
- Evolution of context dependent regulation by expansion of feast/famine regulatory proteins.BMC systems biology · 2014Article
- Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family.Nucleic acids research · 2014Article
- The solution structure of the regulatory domain of tyrosine hydroxylase.Journal of molecular biology · 2014Article
- Cloning, overexpression, purification and preliminary X-ray analysis of a feast/famine regulatory protein (Rv2779c) from Mycobacterium tuberculosis H37Rv.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Abstract
The LrpA protein from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of which the Escherichia coli leucine-responsive regulatory protein is the archetype. Its crystal structure has been determined at 2.9 A resolution and is the first for a member of the Lrp/AsnC family, as well as one of the first for a transcriptional regulator from a hyperthermophile. The structure consists of an N-terminal domain containing a helix-turn-helix (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta character reminiscent of a number of RNA- and DNA-binding domains. Pyrococcus furiosus LrpA forms a homodimer mainly through interactions between the antiparallel beta-sheets of the C-terminal domain, and further interactions lead to octamer formation. The LrpA structure suggests how the protein might bind and possibly distort its DNA substrate through use of its HtH motifs and control gene expression. A possible location for an effector binding site is proposed by using sequence comparisons with other members of the family coupled to mutational analysis.
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