Crystallization of the Oct-1/SNAP190 peptide/DNA complex

Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):511-2. doi: 10.1107/s0907444901021461. Epub 2002 Feb 21.

Abstract

Crystals of the Oct-1 POU/SNAP190 peptide/DNA tertiary complex have been obtained by hanging-drop vapor diffusion at 293K in 20% 2-propanol, 20% PEG 4000 and 0.1M sodium citrate pH 5.6. The Oct-1 POU protein has two domains, one a homeodomain and the other a POU domain, which are connected by a flexible linker. The DNA used in the complex is slightly different in the octamer region compared with the two previously crystallized Oct-1 POU/DNA complexes. The DNA is 14 base pairs, with an octamer sequence of 5'-ATGTAGAT-3' and an overhang of one base on both strands. The SNAP190 peptide is 27 amino acids long (residues 884-910). The crystals diffract to 2.3 A (94.1% completeness) at the synchrotron under cryogenic (123K) conditions. The crystals are triclinic, space group P1, with unit-cell parameters a = 36.4, b = 54.9, c = 77.6A, alpha = 94.9, beta = 99.6, gamma = 109.2 degrees. This structure will provide insight into how Oct-1 interacts with SNAP190, a critical component of the small nuclear RNA-activating protein complex (SNAPc). Transcription of human snRNA genes is activated by these direct protein-protein interactions.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • DNA / chemistry*
  • DNA-Binding Proteins / chemistry*
  • Escherichia coli / chemistry*
  • Host Cell Factor C1
  • Models, Molecular
  • Nucleic Acid Conformation
  • Octamer Transcription Factor-1
  • Peptide Fragments / chemistry
  • Protein Conformation
  • Transcription Factors / chemistry*

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Host Cell Factor C1
  • Octamer Transcription Factor-1
  • Peptide Fragments
  • SNAPC4 protein, human
  • Transcription Factors
  • DNA