The structure of trp RNA-binding attenuation protein.
The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent beta-sheets in the beta-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan.
Antson
A A
AA
Department of Chemistry, University of York, UK.
Otridge
J
J
Brzozowski
A M
AM
Dodson
E J
EJ
Dodson
G G
GG
Wilson
K S
KS
Smith
T M
TM
Yang
M
M
Kurecki
T
T
Gollnick
P
P
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D009876:Operon; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014364:Tryptophan / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; C079092:MtrB protein, Bacteria; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D014157:Transcription Factors; D014364:Tryptophan