4d4h | pdb_00004d4h

Understanding bi-specificity of A-domains

spinqualitylabelsall models 4d4h, resolution 2.02Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d4h is a 1 chain structure with sequence from Planktothrix agardhii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.019Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0WVH3_PLARU Publication Abstract from PubMed Many biologically active peptide secondary metabolites of bacteria are produced by modular enzyme complexes, the non-ribosomal peptide synthetases. Substrate selection occurs through an adenylation (A) domain, which activates the cognate amino acid with high fidelity. The recently discovered A domain of an Anabaenopeptin synthetase from Planktothrix agardhii (ApnA A1 ) is capable of activating two chemically distinct amino acids (Arg and Tyr). Crystal structures of the A domain reveal how both substrates fit into to binding pocket of the enzyme. Analysis of the binding pocket led to the identification of three residues that are critical for substrate recognition. Systematic mutagenesis of these residues created A domains that were monospecific, or changed the substrate specificity to tryptophan. The non-natural amino acid 4-azidophenylalanine is also efficiently activated by a mutant A domain, thus enabling the production of diversified non-ribosomal peptides for bioorthogonal labeling. Structural Elucidation of the Bispecificity of A Domains as a Basis for Activating Non-natural Amino Acids.,Kaljunen H, Schiefelbein SH, Stummer D, Kozak S, Meijers R, Christiansen G, Rentmeister A Angew Chem Int Ed Engl. 2015 Jun 11. doi: 10.1002/anie.201503275. PMID:26096082 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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