1DM9

HEAT SHOCK PROTEIN 15 KD

1DM9 の概要

• エントリーDOI: 10.2210/pdb1dm9/pdb
• 分子名称: HYPOTHETICAL 15.5 KD PROTEIN IN MRCA-PCKA INTERGENIC REGION, SULFATE ION (3 entities in total)
• 機能のキーワード: heat shock proteins, protein-rna interactions, ribosome, structural genomics
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31634.23

構造登録者

Staker, B.L.,Korber, P.,Bardwell, J.C.A.,Saper, M.A. (登録日: 1999-12-14, 公開日: 2000-02-18, 最終更新日: 2024-02-07)

主引用文献

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

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: 10675344
DOI: 10.1093/emboj/19.4.749

実験手法

X-RAY DIFFRACTION (2 Å)