1pmd | pdb_00001pmd

PENICILLIN-BINDING PROTEIN 2X (PBP-2X)

spinqualitylabelsall models 1pmd, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pmd is a 1 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme.,Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O Nat Struct Biol. 1996 Mar;3(3):284-9. PMID:8605631 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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