Structure of a eukaryotic nonribosomal peptide synthetase adenylation domain that activates a large hydroxamate amino acid in siderophore biosynthesis*

HIGHLIGHTS

• who: T. Verne Lee from the residuesNevertheless, our results demonstrate the specificity of Sid, for AHOs over ornithine or any of the other , common amino acids. The structure of Sid, shows that although the substrate binding pockets of eukaryotic NRPS adenylation domains are constructed along fundamentally similar principles to their prokaryotic counterparts, their elaboration to accommodate more complex substrates is not readily predictable from sequence comparison alone. The low success rate of specificityprediction methods for eukaryotic domains is due to the divergence in their signature sequences from those of prokaryotes. The structure of Sid, therefore provides a . . .
  

   

  

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