PMID:10675344
| Citation |
Staker, BL, Korber, P, Bardwell, JC and Saper, MA (2000) Structure of Hsp15 reveals a novel RNA-binding motif. EMBO J. 19:749-57 |
|---|---|
| Abstract |
We have solved the crystal structure of the heat shock protein Hsp15, a newly isolated and very highly inducible heat shock protein that binds the ribosome. Comparison of its structure with those of two RNA-binding proteins, ribosomal protein S4 and threonyl-tRNA synthetase, reveals a novel RNA-binding motif. This newly recognized motif is remarkably common, present in at least eight different protein families that bind RNA. The motif's surface is populated by conserved, charged residues that define a likely RNA-binding site. An intriguing pattern emerges: stress proteins, ribosomal proteins and tRNA synthetases repeatedly share a conserved motif. This may imply a hitherto unrecognized functional similarity between these three protein classes. |
| Links |
PubMed PMC305613 Online version:10.1093/emboj/19.4.749 |
| Keywords |
Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites; Conserved Sequence; Crystallography, X-Ray; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/genetics; RNA-Binding Proteins/metabolism; Ribosomal Proteins/chemistry; Ribosomal Proteins/genetics; Threonine-tRNA Ligase/chemistry; Threonine-tRNA Ligase/genetics |
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