Structural highlights
Function
[HSLR_ECOLI] Involved in the recycling of free 50S ribosomal subunits that still carry a nascent chain. Binds RNA more specifically than DNA. Binds with very high affinity to the free 50S ribosomal subunit. Does not bind it when it is part of the 70S ribosome.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of Hsp15 reveals a novel RNA-binding motif.,Staker BL, Korber P, Bardwell JC, Saper MA EMBO J. 2000 Feb 15;19(4):749-57. PMID:10675344[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Staker BL, Korber P, Bardwell JC, Saper MA. Structure of Hsp15 reveals a novel RNA-binding motif. EMBO J. 2000 Feb 15;19(4):749-57. PMID:10675344 doi:10.1093/emboj/19.4.749
