Crystallization and preliminary X-ray analysis of phage Mu activator protein C in a complex with promoter DNA.
Bacteriophage Mu C protein is an activator of the four Mu late promoters that drive the expression of genes encoding DNA-modification as well as phage head and tail morphogenesis proteins. This report describes the purification and cocrystallization of wild-type and selenomethionine-substituted C protein with a synthetic late promoter P(sym), together with preliminary X-ray diffraction data analysis using SAD phasing. The selenomethionine peak data set was collected from a single crystal which diffracted to 3.1 A resolution and belonged to space group P4(1) or P4(3), with unit-cell parameters a = 68.9, c = 187.6 A and two complexes per asymmetric unit. The structure will reveal the amino acid-DNA interactions and any conformational changes associated with DNA binding.
Shanmuganatham
Karthik K
KK
Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, TN 38163, USA.
Ravichandran
Manimekalai
M
Howe
Martha M
MM
Park
Hee-Won
HW
D010583:Bacteriophage mu / Q000737:chemistry* / Q000235:genetics; D051778:Basic Helix-Loop-Helix Leucine Zipper Transcription Factors / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D004279:DNA, Viral / Q000737:chemistry* / Q000235:genetics; D011401:Promoter Regions, Genetic / Q000235:genetics; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics
D051778:Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; C090591:C protein, Bacteriophage Mu; D004279:DNA, Viral; D014764:Viral Proteins