ArticleBMC structural biology2009
Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103.
Article in BMC structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 34 citations in OpenAlex.
- Fungal Carbonic Anhydrases: A Systematic Review from Molecular Profiling to Pathogenic Regulation inJournal of fungi (Basel, Switzerland) · 2026Review
- Structural basis of membrane potential coupled vectorial CO₂ hydration by the DAB2 complex in chemolithoautotrophs.Nature communications · 2026Article
- Structural characterization and inhibition of carbonic anhydrase fromJournal of structural biology: X · 2025Article
- Contribution of the Mitochondrial Carbonic Anhydrase (MoCA1) to Conidiogenesis and Pathogenesis inFrontiers in microbiology · 2022Article
- Zeta-carbonic anhydrases show CSComputational and structural biotechnology journal · 2021Article
- Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Cellular Localization of Carbonic Anhydrase Nce103p inInternational journal of molecular sciences · 2020Article
- Crystal structure of carbonic anhydrase CaNce103p from the pathogenic yeast Candida albicans.BMC structural biology · 2018Article
- BetaCavityWeb: a webserver for molecular voids and channels.Nucleic acids research · 2015Article
- MOLE 2.0: advanced approach for analysis of biomacromolecular channels.Journal of cheminformatics · 2013Article
- Gates of enzymes.Chemical reviews · 2013Review
- Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon.Nature · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe carbonic anhydrases (CAs) are involved in inorganic carbon utilization. They have been classified into six evolutionary and structural families: alpha-, beta-, gamma-, delta-, epsilon-, zeta- CAs, with beta-CAs present in higher plants, algae and prokaryotes. The yeast Saccharomyces cerevisiae encodes a single copy of beta-CA Nce103/YNL036W.
resultsWe determined the crystal structure of Nce103 in complex with a substrate analog at 2.04 A resolution. It assembles as a homodimer, with the active site located at the interface between two monomers. At the bottom of the substrate pocket, a zinc ion is coordinated by the three highly conserved residues Cys57, His112 and Cys115 in addition to a water molecule. Residues Asp59, Arg61, Gly111, Leu102, Val80, Phe75 and Phe97 form a tunnel to the bottom of the active site which is occupied by a molecule of the substrate analog acetate. Activity assays of full length and two truncated versions of Nce103 indicated that the N-terminal arm is indispensable.
conclusionThe quaternary structure of Nce103 resembles the typical plant type beta-CAs of known structure, with an N-terminal arm indispensable for the enzymatic activity. Comparative structure analysis enables us to draw a possible tunnel for the substrate to access the active site which is located at the bottom of a funnel-shaped substrate pocket.
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.