3wvn | pdb_00003wvn
Complex structure of VinN with L-aspartate
Structural highlights
FunctionPublication Abstract from PubMedAdenylation enzymes play important roles in the biosynthesis and degradation of primary and secondary metabolites. Mechanistic insights into the recognition of alpha-amino acid substrates have been obtained for alpha-amino acid adenylation enzymes. The Asp residue is invariant and is essential for the stabilization of the alpha-amino group of the substrate. In contrast, the beta-amino acid recognition mechanism of adenylation enzymes is still unclear despite the importance of beta-amino acid activation for the biosynthesis of various natural products. Herein, we report the crystal structure of the stand-alone adenylation enzyme VinN, which specifically activates (2S,3S)-3-methylaspartate (3-MeAsp) in vicenistatin biosynthesis. VinN has an overall structure similar to that of other adenylation enzymes. The structure of the complex with 3-MeAsp revealed that a conserved Asp(230) residue is used in the recognition of the beta-amino group of 3-MeAsp similar to alpha-amino acid adenylation enzymes. A mutational analysis and structural comparison with alpha-amino acid adenylation enzymes showed that the substrate-binding pocket of VinN has a unique architecture to accommodate 3-MeAsp as a beta-amino acid substrate. Thus, the VinN structure allows the first visualization of the interaction of an adenylation enzyme with a beta-amino acid and provides new mechanistic insights into the selective recognition of beta-amino acids in this family of enzymes. The crystal structure of the adenylation enzyme VinN reveals a unique beta-amino acid recognition mechanism.,Miyanaga A, Cieslak J, Shinohara Y, Kudo F, Eguchi T J Biol Chem. 2014 Nov 7;289(45):31448-57. doi: 10.1074/jbc.M114.602326. Epub 2014, Sep 22. PMID:25246523[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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