The structure of the transcriptional antiterminator NusB from Escherichia coli

Nat Struct Biol. 2000 Jun;7(6):470-4. doi: 10.1038/75869.

Abstract

We have determined the solution structure of NusB, a transcription antitermination protein from Escherichia coli. The structure reveals a novel, all alpha-helical protein fold. NusB mutations that cause a loss of function (NusB5) or alter specificity for RNA targets (NusB101) are localized to surface residues and likely affect RNA-protein or protein-protein interactions. Residues that are highly conserved among homologs stabilize the protein core. The solution structure of E. coli NusB presented here resembles that of Mycobacterium tuberculosis NusB determined by X-ray diffraction, but differs substantially from a solution structure of E. coli NusB reported earlier.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Conserved Sequence
  • Crystallography, X-Ray
  • Escherichia coli / chemistry*
  • Escherichia coli / genetics
  • Escherichia coli Proteins*
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation / genetics
  • Mycobacterium tuberculosis / chemistry
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Binding
  • Protein Structure, Secondary
  • RNA / genetics
  • RNA / metabolism
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism
  • Sequence Alignment
  • Solutions
  • Transcription Factors / chemistry*
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • NusB protein, E coli
  • RNA-Binding Proteins
  • Solutions
  • Transcription Factors
  • RNA

Associated data

  • PDB/1EY1