Structures of prokaryotic ribosomal proteins: implications for RNA binding and evolution.
After a long hiatus, the pace of determination of the structures of ribosomal proteins has accelerated dramatically. We discuss here the structures of five ribosomal proteins from Bacillus stearothermophilus: S5, S17, L6, L9, and L14. These structures represent several new motifs. Each of these structures has revealed new insights, and we have developed criteria for recognizing RNA-binding regions of each protein and correlating the structures with such properties as antibiotic resistance. The information here should also prove invaluable in an eventual high-resolution picture of the intact ribosome.
Ramakrishnan
V
V
Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
Davies
C
C
Gerchman
S E
SE
Golden
B L
BL
Hoffmann
D W
DW
Jaishree
T N
TN
Kyila
J H
JH
Porter
S
S
White
S W
SW
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D005075:Biological Evolution; D001411:Geobacillus stearothermophilus / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins