1PMD
PENICILLIN-BINDING PROTEIN 2X (PBP-2X)
Summary for 1PMD
| Entry DOI | 10.2210/pdb1pmd/pdb |
| Descriptor | PEPTIDOGLYCAN SYNTHESIS MULTIFUNCTIONAL ENZYME (1 entity in total) |
| Functional Keywords | peptidoglycan synthesis, resistance, cell wall, transmembrane |
| Biological source | Streptococcus pneumoniae |
| Cellular location | Cell membrane; Single-pass membrane protein: P14677 |
| Total number of polymer chains | 1 |
| Total formula weight | 73919.66 |
| Authors | Pares, S.,Mouz, N.,Dideberg, O. (deposition date: 1996-02-05, release date: 1997-02-05, Last modification date: 2024-02-14) |
| Primary citation | Pares, S.,Mouz, N.,Petillot, Y.,Hakenbeck, R.,Dideberg, O. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat.Struct.Biol., 3:284-289, 1996 Cited by PubMed Abstract: 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. PubMed: 8605631DOI: 10.1038/nsb0396-284 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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