Crystallization and preliminary X-ray analysis of the DNA binding domain of the Hin recombinase with its DNA binding site.
The Hin recombinase catalyzes site-specific inversion of DNA. Chemical and genetic studies on Hin binding to the recombination sites indicates that both major and minor DNA groove interactions are critical. In order to determine the molecular nature of these interactions, we have crystallized a synthetically derived 52 amino acid peptide consisting of the DNA binding domain of Hin with a 14 base-pair oligonucleotide representing a recombination half-site. This communication presents preliminary diffraction and analysis of these cocrystals and a packing model for the complex within the crystal.
Feng
J A
JA
Molecular Biology Institute, University of California, Los Angeles 90024.
Simon
M
M
Mack
D P
DP
Dervan
P B
PB
Johnson
R C
RC
Dickerson
R E
RE
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003460:Crystallization; D004254:DNA Nucleotidyltransferases / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000201:enzymology; D014961:X-Ray Diffraction
D004268:DNA-Binding Proteins; D009838:Oligodeoxyribonucleotides; D010446:Peptide Fragments; D004254:DNA Nucleotidyltransferases; C059997:Hin recombinase