4h6w | pdb_00004h6w

Structure of Prenylagaramide maturation protease PagA

spinqualitylabelsall models 4h6w, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4h6w is a 2 chain structure with sequence from Planktothrix agardhii NIES-596. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.45Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F5B6Y7_PLAAG Publication Abstract from PubMed Cyanobactins, a class of ribosomally encoded macrocylic natural products, are biosynthesized through the proteolytic processing and subsequent N-C macrocylization of ribosomal peptide precursors. Macrocylization occurs through a two-step process in which the first protease (PatA) removes the amino terminal flanking sequence from the precursor to yield a free N terminus of the precursor peptide, and the second protease (PatG) removes the C-terminal flanking sequence and then catalyzes the transamidation reaction to yield an N-C cyclized product. Here, we present the crystal structures of the protease domains of PatA and PatG from the patellamide cluster and of PagA from the prenylagaramide cluster. A comparative structural and biochemical analysis of the transamidating PatG protease reveals the presence of a unique structural element distinct from canonical subtilisin proteases, which may facilitate the N-C macrocylization of the peptide substrate. Structures of cyanobactin maturation enzymes define a family of transamidating proteases.,Agarwal V, Pierce E, McIntosh J, Schmidt EW, Nair SK Chem Biol. 2012 Nov 21;19(11):1411-22. doi: 10.1016/j.chembiol.2012.09.012. PMID:23177196 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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