6Y04

Crystal structure of beta-carbonic anhydrase isoform I (TvaCA1) from the Trichomonas vaginalis protozoan.

Summary for 6Y04

• Entry DOI: 10.2210/pdb6y04/pdb
• Descriptor: Carbonic anhydrase, ZINC ION (3 entities in total)
• Functional Keywords: druggable enzyme, lyase
• Biological source: Trichomonas vaginalis
• Total number of polymer chains: 2
• Total formula weight: 40032.86

Authors

Di Fiore, A.,De Simone, G. (deposition date: 2020-02-06, release date: 2020-07-08, Last modification date: 2024-01-24)

Primary citation

Urbanski, L.J.,Di Fiore, A.,Azizi, L.,Hytonen, V.P.,Kuuslahti, M.,Buonanno, M.,Monti, S.M.,Angeli, A.,Zolfaghari Emameh, R.,Supuran, C.T.,De Simone, G.,Parkkila, S.
Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase fromTrichomonas vaginalis.
J Enzyme Inhib Med Chem, 35:1292-1299, 2020

PubMed Abstract: We report the biochemical and structural characterisation of a beta-carbonic anhydrase (β-CA) from , a unicellular parasite responsible for one of the world's leading sexually transmitted infections, trichomoniasis. CAs are ubiquitous metalloenzymes belonging to eight evolutionarily divergent groups (α, β, γ, δ, ζ, η, θ, and ι); humans express only α-CAs, whereas many clinically significant pathogens express only β- and/or γ-CAs. For this reason, the latter two groups of CAs are promising biomedical targets for novel antiinfective agents. The β-CA from (TvaCA1) was recombinantly produced and biochemically characterised. The crystal structure was determined, revealing the canonical dimeric fold of β-CAs and the main features of the enzyme active site. The comparison with the active site of human CA enzymes revealed significant differences that can be exploited for the design of inhibitors selective for the protozoan enzyme with respect to the human ones.

PubMed: 32515610
DOI: 10.1080/14756366.2020.1774572

Experimental method

X-RAY DIFFRACTION (2.48 Å)