Sandbox Reserved 110

This Sandbox is Reserved from May 18 through July 31, 2015 for use in the workshop Protein 3D Structure Visualization & Structural Bioinformatics taught by Eric Martz and Fadel Samatey at the Okinawa Institute of Science and Technology, Japan. This reservation includes Sandbox Reserved 101 through Sandbox Reserved 150. See Workshops.MolviZ.Org.

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Crystal structure of MraY bound to carbacaprazamycin

spinqualitylabelsall models Aricept bound to AChE Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Introduction MraY, called also phospho-N-acetylmuramoyl-pentapeptide-transferase or UDP-MurNAc-pentapeptide phosphotransferase, is an integral membrane enzyme involved in peptidoglycan biosynthesis .MraY is encoded by the mraY gene and belongs to a subfamily of the polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase (PNPT) superfamily . MRAY is a promising candidate for the development of new antibiotics. In fact, it is the target of five classes of natural nucleoside inhibitors with potent antibacterial activity . The structure presented in this page correspond to the MraY protein isolated from Aquifex aeolicus (strain VF5) in complex with carbacaprazamycin Aricept docked onto AChE Function MraY is a critical enzyme in peptidoglycan biosynthesis. Peptidoglycan is an essential component of the cell wall of Gramnegative and Gram-positive bacteria . The cell wall provides bacteria a structural support and protection. In particular, it allows bacteria to maintain their cell shape at different osmotic pressures . Peptidoglycan is a cross-linked polymer of carbohydrates an amino acids and due to its biological relevance in Bacteria, it has been a major target for antibiotics . Peptidoglycan biosynthesis involves three main stages. MraY is responsible for the second stage. First, the peptidoglycan precursor UDP-Nacetylmuramoyl (MurNAc)–pentapeptide is synthesized in the cytosol. Second, this hydrophilic precursor is attached to a lipid carrier, and the complex lipid carrier-precursor is transported, through the membrane, to the periplasm. Third, the peptidoglycan precursors are polymerized to form the cell wall. MraY catalyzes the transfer of phospho-MurNAc-pentapeptide from hydrophilic substrate UDP-MurNAc-pentapeptide to the lipid carier (C55-P) in the presence of a Mg2+ cofactor. The product is the undecaprenyl-pyrophosphoryl-MurNAcpentapeptide, also known as lipid I . Structure MraY is a membrane-bound enzyme, for which the N and the C termini are located on the periplasmic side. This protein is made of four extracellular loops, five cytoplasmic loops (named A,B … and E) and ten transmembrane helices named TM1 to TM10. Though, TM9 is cleaved by a glycin residue into two helical segments named TM9a and TM9b. Furthermore, there is an additional helix between TM9b and TM10, which is only 11 residues long and is called TM9c. This helix contains a HHH motif (H290, 291 and 292) which plays a role in the enzyme’s substrat selectivity and is a part of the catalytic site [1]. For example; they interact with tunicamycin and MD2. This small loop binds two Ni2+ ions, one on the two first histidines and the other one on the last one. Another part of this site is the residues corresponding to Asp117 and Asp118 which are involved in Mg2+coordination [4].TM5–TM10 and loops C and D also play a role in the catalytic site and contain many polar and charged amino acids residues[1]. Also, some polar and charged amino acids on TM9b and loop E are pointing toward the active site, making it even more hydrophilic [4]. 3D related structures 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.