4.2 Article

Expression, Purification, Crystallization and Preliminary X-Ray Crystallographic Analysis of the Peptidoglycan Binding Region of the Ser/Thr Kinase PrkC from Staphylococcus aureus

Journal

PROTEIN AND PEPTIDE LETTERS
Volume 17, Issue 10, Pages 1296-1299

Publisher

BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986610792231401

Keywords

Crystal; cell wall; X-ray; latency

Funding

  1. MIUR [RBRN07BMCT]

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PrkC is an important Ser/Thr membrane kinase of Staphylococcus aureus able to bind peptidoglycans through extra-cellular domains, denominated as PASTA. Upon peptidoglycan binding, PrkC is activated and stimulates bacterial growth and revival from latency. The entire extra-cellular region of PrkC (residues 378-664), containing three predicted PASTA domains and an extra-domain of unknown function, has been successfully crystallized using vapor-diffusion methods. The structure has been solved by Multiwavelength Anomalous Dispersion and refinement is in progress.

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