Open AccessPreliminary crystallography confirms that the archaeal DNA‐binding and tryptophan‐sensing regulator TrpY is a dimer
Author(s) -
Cafasso Jacquelyn,
Manjasetty Babu A.,
Karr Elizabeth A.,
Sandman Kathleen,
Chance Mark R.,
Reeve John N.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110036031
Subject(s) - dimer , crystallography , tryptophan , chemistry , dna , tetragonal crystal system , helix bundle , stereochemistry , transcription (linguistics) , operon , amino acid , biochemistry , protein structure , crystal structure , gene , escherichia coli , organic chemistry , philosophy , linguistics
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 P 4 3 2 1 2 or P 4 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.