1pmd
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(New page: 200px<br /><applet load="1pmd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pmd, resolution 3.5Å" /> '''PENICILLIN-BINDING PR...)
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Revision as of 21:48, 20 November 2007
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PENICILLIN-BINDING PROTEIN 2X (PBP-2X)
Overview
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.
About this Structure
1PMD is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
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
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