ArticleProtein science : a publication of the Protein Society2001
Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 155 citations in OpenAlex.
- Bacterial β-carbonic anhydrases: a six-step prioritization framework for antibacterial target validation.Archives of microbiology · 2026Review
- Multi-faceted exploration of the novel active γ-carbonic anhydrase PaCAγ1 in the human pathogen Pseudomonas aeruginosa.International journal of biological macromolecules · 2025Article
- A Deep Retrieval-Enhanced Meta-Learning Framework for Enzyme Optimum pH Prediction.Journal of chemical information and modeling · 2025Article
- Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Paradigms of convergent evolution in enzymes.The FEBS journal · 2025Article
- Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP.Science advances · 2024Article
- Chemoproteomics Reveals Disruption of Metal Homeostasis and Metalloproteins by the Antibiotic Holomycin.ACS chemical biology · 2023Article
- Investigation of the presence of Capnophilic bacteria in routine urine cultures.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2023Article
- Carbonic Anhydrase Inhibitors as Novel Antibacterials in the Era of Antibiotic Resistance: Where Are We Now?Antibiotics (Basel, Switzerland) · 2023Review
- The gram-negative bacteriumJournal of enzyme inhibition and medicinal chemistry · 2022Article
- Activation studies with amino acids and amines of a β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2022Article
- Contribution of the Mitochondrial Carbonic Anhydrase (MoCA1) to Conidiogenesis and Pathogenesis inFrontiers in microbiology · 2022Article
- Scaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis.Nature structural & molecular biology · 2021Article
- Carbonic Anhydrases: New Perspectives on Protein Functional Role and Inhibition inFrontiers in microbiology · 2021Review
- Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Article
- Activation studies of the β-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Mobility of Lewis acids within the secondary coordination sphere: toward a model for cooperative substrate binding.Chemical communications (Cambridge, England) · 2020Article
- The Effect of Substituted Benzene-Sulfonamides and Clinically Licensed Drugs on the Catalytic Activity of CynT2, a Carbonic Anhydrase Crucial forInternational journal of molecular sciences · 2020Article
- Anion Inhibition Studies of the Beta-Carbonic Anhydrase fromMolecules (Basel, Switzerland) · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Carbonic anhydrases fall into three distinct evolutionary and structural classes: alpha, beta, and gamma. The beta-class carbonic anhydrases (beta-CAs) are widely distributed among higher plants, simple eukaryotes, eubacteria, and archaea. We have determined the crystal structure of ECCA, a beta-CA from Escherichia coli, to a resolution of 2.0 A. In agreement with the structure of the beta-CA from the chloroplast of the red alga Porphyridium purpureum, the active-site zinc in ECCA is tetrahedrally coordinated by the side chains of four conserved residues. These results confirm the observation of a unique pattern of zinc ligation in at least some beta-CAS: The absence of a water molecule in the inner coordination sphere is inconsistent with known mechanisms of CA activity. ECCA activity is highly pH-dependent in the physiological range, and its expression in yeast complements an oxygen-sensitive phenotype displayed by a beta-CA-deletion strain. The structural and biochemical characterizations of ECCA presented here and the comparisons with other beta-CA structures suggest that ECCA can adopt two distinct conformations displaying widely divergent catalytic rates.
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