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Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1067-9. Epub 2003 May 23.

Structural studies of the transpeptidase domain of PBP1a from Streptococcus pneumoniae.

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Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel (CEA/CNRS/UJF), 41 Rue Jules Horowitz, 38027 Grenoble, France.


The synthesis of the bacterial cell wall requires enzymes which are localized both in the cytoplasm and in the periplasm. Penicillin-binding proteins (PBPs) catalyze the last, crucial steps in peptidoglycan biosynthesis and several of them are essential for bacterial survival. High-molecular-mass PBPs can be bifunctional (class A) or monofunctional (class B) and to date no structural information on any class A PBP is available. To initiate the determination of the three-dimensional structure of a class A PBP, crystals of the transpeptidase domain of PBP1a from Streptococcus pneumoniae were prepared by limited proteolysis of the full-length molecule and purification by anion-exchange chromatography and gel filtration. The samples crystallize in space group C222(1), contain one molecule per asymmetric unit and diffract X-rays to 2.7 A. Selenomethionine-labelled crystals have been prepared and structure solution is under way.

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