The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence identity with any member of this enzyme family, the residues involved in substrate-recognition and catalysis are highly conserved in NP_344798.1. NMR studies showed binding affinity of NP_344798.1 for nucleotides and revealed ?s to ms time scale rate processes involving residues constituting the active site. The results thus obtained indicate large-amplitude rearrangements of regular secondary structures facilitate the penetration of the substrate into the occluded nucleotide-binding site of NP_344798.1 and, by inference based on sequence and structural homology, probably a wide range of other nucleotide-adding enzymes. This article is protected by copyright. All rights reserved.
[NMR paper] NMR-based structural analysis of threonylcarbamoyl-AMP synthase and its substrate interactions.
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NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
Linear Mode
