Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis

EMBO J. 1997 Aug 15;16(16):5030-6. doi: 10.1093/emboj/16.16.5030.

Abstract

SacY belongs to a family of, at present, seven bacterial transcriptional antiterminators. The RNA-binding and antitermination capacity of SacY resides in the 55 amino acids at the N-terminal [SacY(1-55)]. The crystal structure at 2 A resolution shows that SacY(1-55) forms a dimer in the crystal, in accordance with the NMR solution structure. The structure of the monomer is a four-stranded beta-sheet with a simple beta1beta2beta3beta4 topology. One side of the sheet is covered by a long surface loop and the other side forms the dimer interface. The dimer is stabilized by the orthogonal stacking of the two beta-sheets. The crystal structure is in excellent agreement with the NMR solution structure (r.m.s. distance for C alpha coordinates is 1.3 A). The structure of SacY(1-55) reveals a new RNA-binding motif.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / chemistry*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Crystallography, X-Ray
  • Dimerization
  • Escherichia coli / genetics
  • Gene Expression / genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Conformation*
  • Protein Structure, Secondary
  • RNA, Bacterial / chemistry
  • RNA, Bacterial / metabolism*
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Transcription Factors*

Substances

  • Bacterial Proteins
  • RNA, Bacterial
  • RNA-Binding Proteins
  • Recombinant Proteins
  • SacY protein, Bacillus subtilis
  • Transcription Factors
  • antiterminator proteins, Bacteria