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

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Abstract:

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.





Keywords: Crystal; X-ray; cell wall; latency

Document Type: Research Article

Publication date: 2010-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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