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Crystallization and preliminary X-ray diffraction studies of the pneumococcal teichoic acid phosphorylcholine esterase Pce.

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.

SUBMITTER: Lagartera L

PROVIDER: S-EPMC1952259 | biostudies-literature | 2005 Feb

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction studies of the pneumococcal teichoic acid phosphorylcholine esterase Pce.

Lagartera Laura L González Ana A Stelter Meike M García Pedro P Kahn Richard R Menéndez Margarita M Hermoso Juan A JA

Acta crystallographica. Section F, Structural biology and crystallization communications 20050201 Pt 2

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-HPDO ...[more]

PMID: 16511000

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Attachment of phosphorylcholine residues to pneumococcal teichoic acids and modification of substitution patterns by the phosphorylcholine esterase.

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