NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes

Biswaranjan Mohanty, Michael Geralt, Kurt Wüthrich, Pedro Serrano

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1 Citation (Scopus)

Abstract

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 μs to ms time scale rate processes involving residues constituting the active site. The results thus obtained indicate that 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.

Original languageEnglish
Pages (from-to)917-925
Number of pages9
JournalProtein Science
Volume25
Issue number4
DOIs
Publication statusPublished - 1 Apr 2016
Externally publishedYes

Keywords

  • DUF925
  • nucleotide-binding protein
  • PF06042
  • protein dynamics
  • protein structure
  • solution NMR

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