Cloning, expression, purification, crystallization and preliminary X-ray analysis of the pilus-associated sortase C from Streptococcus pneumoniae.
The pilus-associated sortase C from Streptococcus pneumoniae (SrtC or Srt-2) acts as a polymerase for the pilus subunit proteins RrgA and RrgB. Here, the crystallization and preliminary X-ray diffraction analysis of three crystal forms of SrtC are reported. One crystal form belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 48.9, b = 96.9, c = 98.9 A, alpha = beta = gamma = 90 degrees . The other two crystal forms belong to space group P222, with unit-cell parameters a = 48.8, b = 97.2, c = 99.2 A, alpha = beta = gamma = 90 degrees and a = 48.6, b = 96.5, c = 98.8 A, alpha = beta = gamma = 90 degrees , respectively. Preliminary analysis indicates the presence of two molecules in the asymmetric unit of the crystal for all three forms.
Neiers
F
F
Department of Bacteriology, Swedish Institute for Infectious Disease Control, Solna.
Madhurantakam
C
C
Fälker
S
S
Normark
S
S
Henriques-Normark
B
B
Achour
A
A
D019881:Aminoacyltransferases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D004058:Diffusion; D004591:Electrophoresis, Polyacrylamide Gel; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D015233:Models, Statistical; D013296:Streptococcus pneumoniae / Q000201:enzymology*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; C509822:sortase C; D019881:Aminoacyltransferases; D003546:Cysteine Endopeptidases