1DM9
HEAT SHOCK PROTEIN 15 KD
Summary for 1DM9
| Entry DOI | 10.2210/pdb1dm9/pdb |
| Descriptor | HYPOTHETICAL 15.5 KD PROTEIN IN MRCA-PCKA INTERGENIC REGION, SULFATE ION (3 entities in total) |
| Functional Keywords | heat shock proteins, protein-rna interactions, ribosome, structural genomics |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 31634.23 |
| Authors | Staker, B.L.,Korber, P.,Bardwell, J.C.A.,Saper, M.A. (deposition date: 1999-12-14, release date: 2000-02-18, Last modification date: 2024-02-07) |
| Primary citation | Staker, B.L.,Korber, P.,Bardwell, J.C.,Saper, M.A. Structure of Hsp15 reveals a novel RNA-binding motif. EMBO J., 19:749-757, 2000 Cited by PubMed 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. PubMed: 10675344DOI: 10.1093/emboj/19.4.749 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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