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• W2040561914 abstract "Sortases are cell-membrane-anchored cysteine transpeptidases that are essential for the assembly and anchoring of cell-surface adhesins in Gram-positive bacteria. Thus, they play critical roles in virulence, infection and colonization by pathogens. Sortases have been classified into four types based on their primary sequence and the target-protein motifs that they recognize. All Gram-positive bacteria express a class A housekeeping sortase (SrtA). Sortase A from Streptococcus pneumoniae (NP_358691) has been crystallized in two crystal forms. Diamond-shaped crystals of ΔN59SrtA diffracted to 4.0 Å resolution and belonged to a tetragonal system with unit-cell parameters a = b = 122.8, c = 86.5 Å, α = β = γ = 90°, while rod-shaped crystals of ΔN81SrtA diffracted to 2.91 Å resolution and belonged to the monoclinic space group P21 with unit-cell parameters a = 66.8, b = 103.47, c = 74.79 Å, α = γ = 90, β = 115.65°. The Matthews coefficient (VM = 2.77 Å3 Da−1) with ∼56% solvent content suggested the presence of four molecules in the asymmetric unit for ΔN81SrtA. Also, a multi-copy search using a monomer as a probe in the molecular-replacement method resulted in the successful location of four sortase molecules in the asymmetric unit, with statistics R = 41.61, Rfree = 46.44, correlation coefficient (CC) = 64.31, CCfree = 57.67." @default.
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• W2040561914 date "2011-09-24" @default.
• W2040561914 modified "2023-09-23" @default.
• W2040561914 title "Crystallization and preliminary X-ray diffraction studies of sortase A from<i>Streptococcus pneumoniae</i>" @default.
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• W2040561914 doi "https://doi.org/10.1107/s1744309111029952" @default.
• W2040561914 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3212360" @default.
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