3wvq

Structure of ATP grasp protein

spinqualitylabelsall models 3wvq, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wvq is a 4 chain structure with sequence from Streptomyces cirratus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.955Å Ligands: GOL, MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0A6YVN3_9ACTN Publication Abstract from PubMed Peptide antibiotics are typically biosynthesized by one of two distinct machineries in a ribosome-dependent or ribosome-independent manner. Pheganomycin (PGM (1)) and related analogs consist of the nonproteinogenic amino acid (S)-2-(3,5-dihydroxy-4-hydroxymethyl)phenyl-2-guanidinoacetic acid (2) and a proteinogenic core peptide, making their origin uncertain. We report the identification of the biosynthetic gene cluster from Streptomyces cirratus responsible for PGM production. Unexpectedly, the cluster contains a gene encoding multiple precursor peptides along with several genes plausibly encoding enzymes for the synthesis of amino acid 2. We identified PGM1, which has an ATP-grasp domain, as potentially capable of linking the precursor peptides with 2, and validate this hypothesis using deletion mutants and in vitro reconstitution. We document PGM1's substrate permissivity, which could be rationalized by a large binding pocket as confirmed via structural and mutagenesis experiments. This is to our knowledge the first example of cooperative peptide synthesis achieved by ribosomes and peptide ligases using a peptide nucleophile. A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin.,Noike M, Matsui T, Ooya K, Sasaki I, Ohtaki S, Hamano Y, Maruyama C, Ishikawa J, Satoh Y, Ito H, Morita H, Dairi T Nat Chem Biol. 2015 Jan;11(1):71-6. doi: 10.1038/nchembio.1697. Epub 2014 Nov 24. PMID:25402768 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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