Crystallization and preliminary X-ray diffraction studies of sortase A from Streptococcus pneumoniae.

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 ΔN(59)SrtA 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 ΔN(81)SrtA diffracted to 2.91 Å resolution and b

SUBMITTER: Misra A 

PROVIDER: S-EPMC3212360 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature