Abstract
The pneumococcal phosphorylcholine esterase (Pce or CbpE) is a modular protein that hydrolyses the phosphorylcholine residues present in the teichoic and lipoteichoic acids of the pneumococcal cell wall. Pce has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality monoclinic crystals belong to space group C2, with unit-cell parameters a = 169.82, b = 57.26, c = 67.44 A, beta = 112.60 degrees. A 2.7 A resolution SAD data set from a non-isomorphous Gd-HPDO3A Pce derivative was collected at the gadolinium L(III) absorption edge using synchrotron radiation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Carboxylic Ester Hydrolases / chemistry*
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Carboxylic Ester Hydrolases / genetics
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Carboxylic Ester Hydrolases / isolation & purification
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Polymerase Chain Reaction
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Restriction Mapping
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Sequence Deletion
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Streptococcus pneumoniae / enzymology*
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X-Ray Diffraction
Substances
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Peptide Fragments
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Recombinant Proteins
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Carboxylic Ester Hydrolases
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teichoic acid phosphorylcholine esterase