1qme: Difference between revisions
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==Overview== | ==Overview== | ||
Penicillin-binding proteins (PBPs), the primary targets for beta-lactam, antibiotics, are periplasmic membrane-attached proteins responsible for, the construction and maintenance of the bacterial cell wall. Bacteria have, developed several mechanisms of resistance, one of which is the mutation, of the target enzymes to reduce their affinity for beta-lactam, antibiotics. Here, we describe the structure of PBP2x from Streptococcus, pneumoniae determined to 2.4 A. In addition, we also describe the PBP2x, structure in complex with cefuroxime, a therapeutically relevant, antibiotic, at 2.8 A. Surprisingly, two antibiotic molecules are observed:, one as a covalent complex with the active-site serine residue, and a, second one between the C-terminal and the transpeptidase domains. The, structure .. | Penicillin-binding proteins (PBPs), the primary targets for beta-lactam, antibiotics, are periplasmic membrane-attached proteins responsible for, the construction and maintenance of the bacterial cell wall. Bacteria have, developed several mechanisms of resistance, one of which is the mutation, of the target enzymes to reduce their affinity for beta-lactam, antibiotics. Here, we describe the structure of PBP2x from Streptococcus, pneumoniae determined to 2.4 A. In addition, we also describe the PBP2x, structure in complex with cefuroxime, a therapeutically relevant, antibiotic, at 2.8 A. Surprisingly, two antibiotic molecules are observed:, one as a covalent complex with the active-site serine residue, and a, second one between the C-terminal and the transpeptidase domains. The, structure of PBP2x reveals an active site similar to those of the class A, beta-lactamases, albeit with an absence of unambiguous deacylation, machinery. The structure highlights a few amino acid residues, namely, Thr338, Thr550 and Gln552, which are directly related to the resistance, phenomenon. | ||
==About this Structure== | ==About this Structure== | ||
1QME is a | 1QME is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: SER. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QME OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
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Revision as of 16:24, 5 November 2007
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PENICILLIN-BINDING PROTEIN 2X (PBP-2X)
OverviewOverview
Penicillin-binding proteins (PBPs), the primary targets for beta-lactam, antibiotics, are periplasmic membrane-attached proteins responsible for, the construction and maintenance of the bacterial cell wall. Bacteria have, developed several mechanisms of resistance, one of which is the mutation, of the target enzymes to reduce their affinity for beta-lactam, antibiotics. Here, we describe the structure of PBP2x from Streptococcus, pneumoniae determined to 2.4 A. In addition, we also describe the PBP2x, structure in complex with cefuroxime, a therapeutically relevant, antibiotic, at 2.8 A. Surprisingly, two antibiotic molecules are observed:, one as a covalent complex with the active-site serine residue, and a, second one between the C-terminal and the transpeptidase domains. The, structure of PBP2x reveals an active site similar to those of the class A, beta-lactamases, albeit with an absence of unambiguous deacylation, machinery. The structure highlights a few amino acid residues, namely, Thr338, Thr550 and Gln552, which are directly related to the resistance, phenomenon.
About this StructureAbout this Structure
1QME is a Single protein structure of sequence from Streptococcus pneumoniae with SO4 as ligand. Structure known Active Site: SER. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance., Gordon E, Mouz N, Duee E, Dideberg O, J Mol Biol. 2000 Jun 2;299(2):477-85. PMID:10860753
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