ArticleThe Journal of biological chemistry2015
Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- Novel binding partners of the Vacuolar Transporter Chaperone (VTC) complex in Acidocalcisomes of Leishmania tarentolae.PLoS neglected tropical diseases · 2026Article
- QuantumPDB: A Workflow for High-Throughput Quantum Cluster Model Generation from Protein Structures.Journal of chemical information and modeling · 2026Article
- Possible Role of CHAD Proteins in Copper Resistance.Microorganisms · 2024Article
- A Class IV Adenylate Cyclase, CyaB, Is Required for Capsule Polysaccharide Production and Biofilm Formation in Vibrio parahaemolyticus.Applied and environmental microbiology · 2023Article
- Inorganic polyphosphate abets silencing of a sub-telomeric gene cluster in fission yeast.microPublication biology · 2023Article
- Article
- Pull-Down Into Active Inclusion Bodies and Their Application in the Detection of (Poly)-Phosphates and Metal-Ions.Frontiers in bioengineering and biotechnology · 2022Article
- On the nature of thiamine triphosphate in Arabidopsis.Plant direct · 2020Article
- Crystal structures of the RNA triphosphatase fromThe Journal of biological chemistry · 2020Article
- Identity and functions of inorganic and inositol polyphosphates in plants.The New phytologist · 2020Review
- Molecular characterization of CHAD domains as inorganic polyphosphate-binding modules.Life science alliance · 2019Article
- Concerted expression of a cell cycle regulator and a metabolic enzyme from a bicistronic transcript in plants.Nature plants · 2019Article
- The macro domain as fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2017Article
- mRNA capping: biological functions and applications.Nucleic acids research · 2016Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
Abstract
Triphosphate tunnel metalloenzymes (TTMs) are present in all kingdoms of life and catalyze diverse enzymatic reactions such as mRNA capping, the cyclization of adenosine triphosphate, the hydrolysis of thiamine triphosphate, and the synthesis and breakdown of inorganic polyphosphates. TTMs have an unusual tunnel domain fold that harbors substrate- and metal co-factor binding sites. It is presently poorly understood how TTMs specifically sense different triphosphate-containing substrates and how catalysis occurs in the tunnel center. Here we describe substrate-bound structures of inorganic polyphosphatases from Arabidopsis and Escherichia coli, which reveal an unorthodox yet conserved mode of triphosphate and metal co-factor binding. We identify two metal binding sites in these enzymes, with one co-factor involved in substrate coordination and the other in catalysis. Structural comparisons with a substrate- and product-bound mammalian thiamine triphosphatase and with previously reported structures of mRNA capping enzymes, adenylate cyclases, and polyphosphate polymerases suggest that directionality of substrate binding defines TTM catalytic activity. Our work provides insight into the evolution and functional diversification of an ancient enzyme family.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.