H. Vantilbeurgh et al., CRYSTAL-STRUCTURE OF A NEW RNA-BINDING DOMAIN FROM THE ANTITERMINATORPROTEIN SACY OF BACILLUS-SUBTILIS, EMBO journal, 16(16), 1997, pp. 5030-5036
SacY belongs to a family of, at present, seven bacterial transcription
al antiterminators. The RNA-binding and antitermination capacity of Sa
cY resides in the 55 amino acids at the N-terminal [SacY(1-55)]. The c
rystal structure at 2 Angstrom resolution shows that SacY(1-55) forms
a dimer in the crystal, in accordance with the NMR solution structure,
The structure of the monomer is a four-stranded beta-sheet with a sim
ple beta 1 beta 2 beta 3 beta 4 topology, One side of the sheet is cov
ered by a long surface loop and the other side forms the dimer interfa
ce. The dimer is stabilized by the orthogonal stacking of the tyro bet
a-sheets, The crystal structure is in excellent agreement with the NMR
solution structure (r.m.s. distance for C alpha coordinates is 1.3 An
gstrom), The structure of SacY(1-55) reveals a new RNA-binding motif.