Preliminary crystallography confirms that the archaeal DNA-binding and tryptophan-sensing regulator TrpY is a dimer.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 11): 1493-5, 2010 Nov 01.
Article
in En
| MEDLINE
| ID: mdl-21045304
ABSTRACT
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 = 147â
Å, and diffracted to 2.9â
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Methanobacteriaceae
/
Archaeal Proteins
/
DNA-Binding Proteins
/
Protein Multimerization
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2010
Document type:
Article
Affiliation country:
United States