Detail Structural Insight into the Transglycosylation Step of Bacterial Cell-Wall Biosynthesis   Oleh:  Lovering, Andrew L. ; De Castro, Liza H ; Lim, Daniel ; Strynadka, Natalie C.J. Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 315 no. 5817 (Mar. 2007), page 1402. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.03 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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