9S4G
Carbonic anhydrases from Candida parapsilosis
Summary for 9S4G
| Entry DOI | 10.2210/pdb9s4g/pdb |
| Descriptor | Carbonic anhydrase, ZINC ION, 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE, ... (4 entities in total) |
| Functional Keywords | carbonic anhydrases, candida parapsilosis, acetazolamide, lyase |
| Biological source | Candida parapsilosis |
| Total number of polymer chains | 4 |
| Total formula weight | 104043.02 |
| Authors | Dostal, J. (deposition date: 2025-07-28, release date: 2025-11-26, Last modification date: 2025-12-17) |
| Primary citation | Dostal, J.,Uhrova, Z.,Skrlova, M.,Machacek, S.,Clarova, K.,Lepsik, M.,Bulvas, O.,Vrabel, M.,Heidingsfeld, O.,Pichova, I. Structural characterization and inhibition of carbonic anhydrase from Candida parapsilosis. J Struct Biol X, 12:100140-100140, 2025 Cited by PubMed Abstract: Fungal carbonic anhydrases (CAs) are metalloenzymes that catalyze the reversible hydration of carbon dioxide and play an essential role in fungal adaptation to environments with fluctuating CO concentrations. The opportunistic pathogen expresses a single β-class CA, CpNce103p, which is structurally distinct from human α-class CAs and therefore may represent a promising antifungal target. Here, we report the biochemical and structural characterization of CpNce103p, including its crystal structure in complex with the classical CA inhibitor acetazolamide. Mass photometry and X-ray crystallography revealed that CpNce103p forms a stable homotetramer, similar to its homolog CaNce103p from . Inhibition constants (Ki) were measured for a panel of 16 sulfonamide derivatives. One compound attained single-digit micromolar inhibition of CpNce103p, similar to the Ki of acetazolamide. Docking suggested the compound's binding mode, featuring zinc coordination and accommodation within the tight cavity. Our findings provide a structural basis for rational inhibitor design targeting fungal β-CAs and support CpNce103p as a viable target for the development of antifungal agents with selective activity. PubMed: 41321686DOI: 10.1016/j.yjsbx.2025.100140 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.701 Å) |
Structure validation
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