3wv4
From Proteopedia
Crystal structure of VinN
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
|