1HK9

Crystal structure of the Hfq protein from Escherichia coli

1HK9 の概要

• エントリーDOI: 10.2210/pdb1hk9/pdb
• 分子名称: PROTEIN HFQ (2 entities in total)
• 機能のキーワード: rna-binding protein, sm-like, pleiotropic regulator, rna binding protein, rna chaperone
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 49545.43

構造登録者

Sauter, C.,Basquin, J.,Suck, D. (登録日: 2003-03-06, 公開日: 2003-07-24, 最終更新日: 2023-12-13)

主引用文献

Sauter, C.,Basquin, J.,Suck, D.
Sm-Like Proteins in Eubacteria: The Crystal Structure of the Hfq Protein from Escherichia Coli
Nucleic Acids Res., 31:4091-, 2003

PubMed Abstract: The Hfq protein was discovered in Escherichia coli in the early seventies as a host factor for the Qbeta phage RNA replication. During the last decade, it was shown to be involved in many RNA processing events and remote sequence homology indicated a link to spliceosomal Sm proteins. We report the crystal structure of the E.coli Hfq protein showing that its monomer displays a characteristic Sm-fold and forms a homo-hexamer, in agreement with former biochemical data. Overall, the structure of the E.coli Hfq ring is similar to the one recently described for Staphylococcus aureus. This confirms that bacteria contain a hexameric Sm-like protein which is likely to be an ancient and less specialized form characterized by a relaxed RNA binding specificity. In addition, we identified an Hfq ortholog in the archaeon Methanococcus jannaschii which lacks a classical Sm/Lsm gene. Finally, a detailed structural comparison shows that the Sm-fold is remarkably well conserved in bacteria, Archaea and Eukarya, and represents a universal and modular building unit for oligomeric RNA binding proteins.

PubMed: 12853626
DOI: 10.1093/NAR/GKG480

実験手法

X-RAY DIFFRACTION (2.15 Å)