ArticleBMC structural biology2007
The crystal structure of Escherichia coli TdcF, a member of the highly conserved YjgF/YER057c/UK114 family.
Article in BMC structural biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 56 citations in OpenAlex.
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- Site-directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus.Protein science : a publication of the Protein Society · 2024Article
- Enhancing coevolutionary signals in protein-protein interaction prediction through clade-wise alignment integration.Scientific reports · 2024Article
- Modulators of a robust and efficient metabolism: Perspective and insights from the Rid superfamily of proteins.Advances in microbial physiology · 2023Review
- Rid7C, a Member of the YjgF/YER057c/UK114 (Rid) Protein Family, Is a Novel Endoribonuclease That Regulates the Expression of a Specialist RNA Polymerase Involved in Differentiation in Nonomuraea gerenzanensis.Journal of bacteriology · 2022Article
- Crystal structure of a hypothetical protein from Giardia lamblia.Acta crystallographica. Section F, Structural biology communications · 2022Article
- RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.Microbiology and molecular biology reviews : MMBR · 2020Review
- Two novel fish paralogs provide insights into the Rid family of imine deaminases active in pre-empting enamine/imine metabolic damage.Scientific reports · 2020Article
- Heat and Pressure Resistance inFrontiers in microbiology · 2020Article
- Reactive Enamines and Imines In Vivo: Lessons from the RidA Paradigm.Trends in biochemical sciences · 2019Review
- Identification of a perchloric acid-soluble protein (PSP)-like ribonuclease from Trichomonas vaginalis.Parasitology research · 2018Article
- A novel chlorination-induced ribonuclease YabJ fromBioscience reports · 2018Article
- Imine Deaminase Activity and Conformational Stability of UK114, the Mammalian Member of the Rid Protein Family Active in Amino Acid Metabolism.International journal of molecular sciences · 2018Article
- Article
- Crystal structures of RidA, an important enzyme for the prevention of toxic side products.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe YjgF/YER057c/UK114 family of proteins is widespread in nature, but has as yet no clearly defined biological role. Members of the family exist as homotrimers and are characterised by intersubunit clefts that are delineated by well-conserved residues; these sites are likely to be of functional significance, yet catalytic activity has never been detected for any member of this family. The gene encoding the TdcF protein of E. coli, a YjgF/YER057c/UK114 family member, resides in an operon that strongly suggests a role in the metabolism of 2-ketobutyrate for this protein.
resultsWe have determined the crystal structure of E. coli TdcF by molecular replacement to a maximum resolution of 1.6 A. Structures are also presented of TdcF complexed with a variety of ligands.
conclusionThe TdcF structure closely resembles those of all YjgF/YER057c/UK114 family members determined thus far. It has the trimeric quaternary structure and intersubunit cavities characteristic of this family of proteins. We show that TdcF is capable of binding several low molecular weight metabolites bearing a carboxylate group, although the interaction with 2-ketobutyrate appears to be the most well defined. These observations may be indicative of a role for TdcF in sensing this potentially toxic metabolite.
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