Preliminary crystallography confirms that the archaeal DNA-binding and tryptophan-sensing regulator TrpY is a dimer.
TrpY regulates the transcription of the metabolically expensive tryptophan-biosynthetic operon in the thermophilic archaeon Methanothermobacter thermautotrophicus. TrpY was crystallized using the hanging-drop method with ammonium sulfate as the precipitant. The crystals belonged to the tetragonal space group P4(3)2(1)2 or P4(1)2(1)2, with unit-cell parameters a = b = 87, c = 147 Å, and diffracted to 2.9 Å resolution. The possible packing of molecules within the cell based on the values of the Matthews coefficient (V(M)) and analysis of the self-rotation function are consistent with the asymmetric unit being a dimer. Determining the structure of TrpY in detail will provide insight into the mechanisms of DNA binding, tryptophan sensing and transcription regulation at high temperature by this novel archaeal protein.
United States Department of Energy Summer Undergraduate Laboratory Intern (SULI), College of Agriculture and Life Sciences, Cornell University, Ithaca, NY 14853, USA.
Jacquelyn
J
Cafasso
Babu A
BA
Manjasetty
Elizabeth A
EA
Karr
Kathleen
K
Sandman
Mark R
MR
Chance
John N
JN
Reeve
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D017013:Methanobacteriaceae / Q000737:chemistry* / Q000378:metabolism; D055503:Protein Multimerization
D019843:Archaeal Proteins; D004268:DNA-Binding Proteins