5ig8

Crystal structure of macrocyclase MdnB from Microcystis aeruginosa MRC

spinqualitylabelsall models 5ig8, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ig8 is a 2 chain structure with sequence from Microcystis aeruginosa MRC. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.278Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B2G3C9_MICAE Publication Abstract from PubMed Macrocyclization is a common feature of natural product biosynthetic pathways including the diverse family of ribosomal peptides. Microviridins are architecturally complex cyanobacterial ribosomal peptides that target proteases with potent reversible inhibition. The product structure is constructed via three macrocyclizations catalyzed sequentially by two members of the ATP-grasp family, a unique strategy for ribosomal peptide macrocyclization. Here we describe in detail the structural basis for the enzyme-catalyzed macrocyclizations in the microviridin J pathway of Microcystis aeruginosa. The macrocyclases MdnC and MdnB interact with a conserved alpha-helix of the precursor peptide using a novel precursor-peptide recognition mechanism. The results provide insight into the unique protein-protein interactions that are key to the chemistry, suggest an origin for the natural combinatorial synthesis of microviridin peptides, and provide a framework for future engineering efforts to generate designed compounds. Structural basis for precursor protein-directed ribosomal peptide macrocyclization.,Li K, Condurso HL, Li G, Ding Y, Bruner SD Nat Chem Biol. 2016 Nov;12(11):973-979. doi: 10.1038/nchembio.2200. Epub 2016 Sep, 26. PMID:27669417 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA