Sandbox Reserved 1488

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Enterococcus faecalis Penicillin Binding Protein 4 (PBP4)

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long-term biochemical experimental investigations, and results from more recent techniques such as protein localization by green fluorescent protein-fusion immunofluorescence or double-hybrid assay, have brought our understanding of the last stages of the peptidoglycan biosynthesis to an outstanding level that allows a broad outlook on the properties of these enzymes. Details are emerging regarding the interaction between the peptidoglycan-synthesizing PBPs and the peptidoglycan, their mesh net-like product that surrounds and protects bacteria. Function The bacterial cell wall is essential for cell survival. It is composed of layers of peptidoglycan modified with proteins and polymers. In bacteria, this peptidoglycan layer is formed by the coordinated action of multiple proteins, including penicillin-binding proteins (PBPs). PBPs are transpeptidases, carboxypeptidases and endopeptidases that synthesize new and remodel existing peptidoglycan. PBPs are classified by their enzymatic activity: (1) class A, bifunctional PBPs with both glycosyltransferase and transpeptidase activities; (2) class B, transpeptidases; and (3) class C, carboxy-peptidases and endopeptidases. Disease Enterococci exhibits tolerance to the bactericidal activity of β-lactams , a phenomenon that compromises the use of β-lactam antibiotics as single agents in the treatment of enterococcal endocarditis . As a consequence, multi-resistant E. faecium and E. faecalis represent one of the most dangerous threats in infectious diseases therapeutics. Rare strains of E. faecalis and most nosocomial strains of E. faecium exhibit even higher levels of resistance to penicillins, effectively eliminating β-lactams as a treatment option . Of greater concern is the observation that prolonged β-lactam therapy can lead to the emergence of highly resistant strains. Structural insights into β-lactam resistance This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.