Work

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

Year: 2016

Type: article

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.

Source: Protein Science

DOI: 10.1002/pro.2872

Authors: Biswaranjan Mohanty, Michael Geralt, Kurt Wüthrich, Pedro Serrano

Institutions: Scripps Research Institute, Joint Center for Structural Genomics

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: Joint Center for Structural Genomics, G4047395780, G9000331358