Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the peptidoglycan binding region of the Ser/Thr kinase PrkC from Staphylococcus aureus

Alessia Ruggiero; Flavia Squeglia; Viviana Izzo; Alba Silipo; Luigi Vitagliano; Antonio Molinaro; Rita Berisio

doi:10.2174/092986610792231401

Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the peptidoglycan binding region of the Ser/Thr kinase PrkC from Staphylococcus aureus

Protein Pept Lett. 2010 Oct;17(10):1296-9. doi: 10.2174/092986610792231401.

Authors

Alessia Ruggiero¹, Flavia Squeglia, Viviana Izzo, Alba Silipo, Luigi Vitagliano, Antonio Molinaro, Rita Berisio

Affiliation

¹ Institute of Biostructures and Bioimaging, CNR, Napoli, Italy.

PMID: 20594157
DOI: 10.2174/092986610792231401

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallography, X-Ray
Peptidoglycan / chemistry*
Peptidoglycan / metabolism
Protein Binding
Protein Serine-Threonine Kinases* / chemistry
Protein Serine-Threonine Kinases* / genetics
Protein Serine-Threonine Kinases* / metabolism
Staphylococcus aureus* / chemistry
Staphylococcus aureus* / genetics
Staphylococcus aureus* / metabolism

Substances

Peptidoglycan
Protein Serine-Threonine Kinases