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3.4.22.B63: sortase C

This is an abbreviated version!
For detailed information about sortase C, go to the full flat file.

Word Map on EC 3.4.22.B63

Reaction

The enzyme from Bacillus anthracis cleaves the LPNT-/-A sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli [17074072]. The enzymes from Streptococcus pneumoniae and Enterococcus faecalis are required for efficient pilus assembly. =

Synonyms

pilus-associated sortase C, sortase C, sortase C1, sortase C2, sortaseC1, Srt-2, SrtC, SrtC-1, SrtC-2, SrtC-3, SrtC1, SrtC2, SrtC_1, SrtC_2, yhhA

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B63 sortase C

Crystallization

Crystallization on EC 3.4.22.B63 - sortase C

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 10% (w/v) PEG monomethyl ether 2000 and 100 mM MES (pH 6.4)
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sitting drop vapor diffusion method, using 100 mM Tris (pH 8.5), 200 mM NaOAc, and 30% (w/v) PEG-4000
apoprotein, hanging drop vapor diffusion method, using 15-25% (w/v) polyethylene glycol 3350 and 0.2 M Tris buffer (pH 8.0-8.8) and 0.2 M ammonium acetate at 4°C. In complex with inhibitor 2-(trimethylammonium)ethyl thiol, hanging drop vapor diffusion method, using 1.6 M ammonium sulfate, 5% (w/v) polyethylene glycol 3350, and sodium cacodylate (pH 6.5) at 4°C
isofofm SrtC1, hanging drop vapor diffusion method, using 0.4 M sodium formate, 0.1 M Bis-Tris propane pH 6.5, and 22% (w/v) PEG 3350. Isoform SrtC1, hanging drop vapor diffusion method, using 0.26 M CaCl2, 19% (w/v) PEG 6000, 0.1 M HEPES pH 7.0
molecular dynamics simulations of SrtC isozymes with the sorting signals of RrgA, RrgB, and RrgC to determine the structural and thermodynamic basis of pilin recognition. Both isozymes SrtC-1 and SrtC-3 are selective for RrgB. This specificity is tuned by the sorting signal binding conformation in which the first two residue side-chains complement hydrophobic residues around the active site, while the third residue projects away from the catalytic triad and makes specific interactions based on its charge and reach
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molecular dynamics simulations of SrtC isozymes with the sorting signals of RrgA, RrgB, and RrgC to determine the structural and thermodynamic basis of pilin recognition. SrtC-2 is selective for RrgA. This specificity is tuned by the sorting signal binding conformation in which the first two residue sidechains complement hydrophobic residues around the active site, while the third residue projects away from the catalytic triad and makes specific interactions based on its charge and reach
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sitting drop vapor diffusion method
three different crystals are obtained using both the sitting-drop and hanging-drop vapour-diffusion methods. The three crystals belonged to different space groups and diffracted to resolutions ranging between 2.3 and 1.7 A. One crystal form belongs to space group P212121, with unit cell parameters a = 48.9, b = 96.9, c = 98.9 A, alpha = beta = gamma = 90°. 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° and a = 48.6, b= 96.5, c = 98.8 A, alpha = beta = gamma = 90°, respectively
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hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 8.5, 0.54 M sodium citrate, 8% (v/v) iso-propanol, 8% (v/v) tert-butanol