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Nat Struct Biol. 1996 Mar;3(3):284-9.

X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme.

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Institut de Biologie Structurale, Laboratoire de Cristallographie Macromoléculaire, Grenoble, France.


All beta-lactam antibiotics exert their biological effects by interacting with a unique class of proteins, the penicillin-binding proteins (PBPs). These membrane proteins are involved in the biosynthesis of the murein or peptidoglycan, a mesh-like structure which completely surrounds the bacterial cell. Sequence similarities indicate that one domain of these proteins belongs to a large family of beta-lactam-recognizing proteins, which includes the active-site serine beta-lactamases. We here report the first three-dimensional crystal structure of a high molecular weight penicillin-binding protein, PBP2x of Streptococcus pneumoniae, at 3.5 A resolution. The molecule has three domains, the central domain being a transpeptidase, which is a suitable target for antibiotic development.

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