Database accession: MF7000856
Name: Beta-carbonic anhydrase isoform I (TvaCA1) (Trichomonas vaginalis protozoan)
PDB ID: 6y04
Experimental method: X-ray (2.48 Å)
Assembly: Homodimer
Source organism: Trichomonas vaginalis
Primary publication of the structure:
Urbański LJ, Di Fiore A, Azizi L, Hytönen VP, Kuuslahti M, Buonanno M, Monti SM, Angeli A, Zolfaghari Emameh R, Supuran CT, De Simone G, Parkkila S
Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from .
(2020) J Enzyme Inhib Med Chem 35: 1292-1299
PMID: 32515610
Abstract:
We report the biochemical and structural characterisation of a beta-carbonic anhydrase (β-CA) from Trichomonas vaginalis, 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 T. vaginalis (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.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
carbonate dehydratase activity carbonate dehydratase activity
zinc ion binding zinc ion binding
Biological process: not assigned
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Carbonic anhydrase
Source organism: Trichomonas vaginalis
Length: 182 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSQLELITSANQAFLEANPELTKLNKAPQRHIAIVTCMDTRLVNFAEDAIGVKRGEATVIKAAGNGIWTTGLSDIVVSLLVSIYELGVQEIFIMGHECCGMTHASTDSLGAQMLKSGIKPEDIEKFKSDLSKWVDDFKDPIDNIKNSVRCVRENPLIPKNIPIHGLLIHPDTGKVTTIINGY
UniProtKB AC: A2ENQ8 (positions: 1-182)
Coverage: 100%
Name: Carbonic anhydrase
Source organism: Trichomonas vaginalis
Length: 182 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSQLELITSANQAFLEANPELTKLNKAPQRHIAIVTCMDTRLVNFAEDAIGVKRGEATVIKAAGNGIWTTGLSDIVVSLLVSIYELGVQEIFIMGHECCGMTHASTDSLGAQMLKSGIKPEDIEKFKSDLSKWVDDFKDPIDNIKNSVRCVRENPLIPKNIPIHGLLIHPDTGKVTTIINGY
UniProtKB AC: A2ENQ8 (positions: 1-182)
Coverage: 100%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Carbonic anhydrase
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The native carbonic anhydrase is dimeric in solution, in agreement with being a tightly associated dimer with a large, hydrophobic buried surface area. The extended β-sheet core consisting of ten β–strands is equally contributed by the two monomers, and the N-terminal helix of each monomer extends around the other monomer. Based on the highly intertwined structure, the monomeric form is most probably not a stable, independently folding unit. The two active sites are also located in clefts at the dimeric interface, further suggesting that dimer is the functional form (PMID:32515610).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
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