Structure of YqgQ protein from Bacillus subtilis, a conserved hypothetical protein

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):8-11. doi: 10.1107/S1744309109047009. Epub 2009 Dec 25.

Abstract

The crystal structure of the hypothetical protein YqgQ from Bacillus subtilis has been determined to 2.1 A resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 51.85, b = 41.25, c = 55.18 A, beta = 113.4 degrees , and contained three protein molecules in the asymmetric unit. The structure was determined by the single-wavelength anomalous dispersion method using selenium-labeled protein and was refined to a final R factor of 24.7% (R(free) = 28.0%). The protein molecule mainly comprises a three-helical bundle. Its putative function is inferred to be single-stranded nucleic acid binding based on sequence and structural homology.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / chemistry*
  • Bacterial Proteins / chemistry*
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Sequence Alignment

Substances

  • Bacterial Proteins

Associated data

  • PDB/2NN4
  • PDB/R2NN4SF