Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/354
Title: Crystallization and preliminary X-ray diffraction studies of sortase A from Streptococcus pneumoniae.
Authors: Suryanarayanarao, Ramakumar
Misra, Anurag
Biswas, Tora
Das, Sreetama
Marathe, Uttara
Devinder Sehgal, Devinder
Roy, Rajendra P
Issue Date: Oct-2011
Publisher: International Union of Crystallography.
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 belonged to the monoclinic space group P2(1) with unit-cell parameters a = 66.8, b = 103.47, c = 74.79 Å, α = γ = 90, β = 115.65°. The Matthews coefficient (V(M) = 2.77 Å(3) Da(-1)) with ~56% solvent content suggested the presence of four molecules in the asymmetric unit for ΔN(81)SrtA. 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, R(free) = 46.44, correlation coefficient (CC) = 64.31, CC(free) = 57.67.
URI: http://hdl.handle.net/123456789/354
Appears in Collections:Molecular Immunology, Publications

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