Literature summary for 3.4.11.9 extracted from

Arreola, R.; Villalpando, J.L.; Puente-Rivera, J.; Morales-Montor, J.; Rudino-Pinera, E.; Alvarez-Sanchez, M.E.
Trichomonas vaginalis metalloproteinase TvMP50 is a monomeric aminopeptidase P-like enzyme (2018), Mol. Biotechnol., 60, 563-575 .

Cloned(Commentary)

Cloned (Comment)	Organism
sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli	Trichomonas vaginalis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His6-tagged enzyme, microbatch crystallization method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of crstallization solution containing 30% v/v PEG400, 0.1 M sodium acetate, 0.2 M calcium acetate, pH 4.5, the pH is adjusted to pH 5.8 with acetic acid, X-ray diffraction structure determination and analysis at 3.4 A, molecular replacement based on the structure of human prolidase (PDB ID 2IW2)	Trichomonas vaginalis

Crystallization (Comment)

Organism

purified recombinant His6-tagged enzyme, microbatch crystallization method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of crstallization solution containing 30% v/v PEG400, 0.1 M sodium acetate, 0.2 M calcium acetate, pH 4.5, the pH is adjusted to pH 5.8 with acetic acid, X-ray diffraction structure determination and analysis at 3.4 A, molecular replacement based on the structure of human prolidase (PDB ID 2IW2)

Trichomonas vaginalis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	enzyme bound	Trichomonas vaginalis
additional information	the active site of each subunit of puified recombinant TVMP50 contains two metals Ca2+ and Ni2+. The Ni2+ is likely also dragged from the IMAC resin purification. Additional Ca2+ atoms are detected bound in the structure, one on the N-terminal and two on the C-terminal domain. The conserved residues responsible for direct interaction with metallic ions are Glu407, Glu364, Asp232, Asp243, His328, and His335	Trichomonas vaginalis

Organism

Organism	UniProt	Comment	Textmining
Trichomonas vaginalis	A2F8Y2	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and ultrafiltration	Trichomonas vaginalis

Subunits

Subunits	Comment	Organism
monomer	1 * 50000, about, mass spectrometry	Trichomonas vaginalis
More	crystallographic coordinates show a monomer on a pseudo-homodimer array on the asymmetric unit that resembles the quaternary structure of the M24B dimeric family and suggests a homodimeric aminopeptidase P-like enzyme as a likely ancestor. TvMP50 has a modified N-terminal region compared with other Xaa-Pro aminopeptidases/prolidases with three-dimensional structures. The formation of the standard dimer is structurally unstable in aqueous solution, and a comparably reduced number of hydrogen bridges and lack of saline bridges are found between subunits A/B, which explain why TvMP50 portrays monomeric functionality	Trichomonas vaginalis

Synonyms

Synonyms	Comment	Organism
aminopeptidase P-like enzyme	-	Trichomonas vaginalis
TvMP50	-	Trichomonas vaginalis

General Information

General Information	Comment	Organism
evolution	the enzyme TvMP50 belong to the aminopeptidase P-like metalloproteinase subfamily A/B, family M24 of clan MG, Parabasalia group. The Parabasalia group contains two protein lineages with a pita bread fold; the ancestral monomeric group 1 is probably derived from an ancestral dimeric aminopeptidase P-type enzyme, and group 2 has a probable dimeric kind of ancestral eukaryotic prolidase lineage. Phylogenetic analysis, overview	Trichomonas vaginalis
additional information	Trichomonas vaginalis metalloproteinase TvMP50 is a monomeric aminopeptidase P-like enzyme	Trichomonas vaginalis