5O5S

X-ray crystal structure of the RapZ C-terminal domain from Escherichia coli

5O5S の概要

• エントリーDOI: 10.2210/pdb5o5s/pdb
• 分子名称: RNase adapter protein RapZ, MALONATE ION (3 entities in total)
• 機能のキーワード: rna binding amino-sugar metabolism kinase like domain pfk like domain, chaperone
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15552.74

構造登録者

Gonzalez, G.M.,Durica-Mitic, S.,Hardwick, S.W.,Moncrieffe, M.,Resch, M.,Neumann, P.,Ficner, R.,Gorke, B.,Luisi, B.F. (登録日: 2017-06-02, 公開日: 2017-08-30, 最終更新日: 2024-05-08)

主引用文献

Gonzalez, G.M.,Durica-Mitic, S.,Hardwick, S.W.,Moncrieffe, M.C.,Resch, M.,Neumann, P.,Ficner, R.,Gorke, B.,Luisi, B.F.
Structural insights into RapZ-mediated regulation of bacterial amino-sugar metabolism.
Nucleic Acids Res., 45:10845-10860, 2017

PubMed Abstract: In phylogenetically diverse bacteria, the conserved protein RapZ plays a central role in RNA-mediated regulation of amino-sugar metabolism. RapZ contributes to the control of glucosamine phosphate biogenesis by selectively presenting the regulatory small RNA GlmZ to the essential ribonuclease RNase E for inactivation. Here, we report the crystal structures of full length Escherichia coli RapZ at 3.40 Å and 3.25 Å, and its isolated C-terminal domain at 1.17 Å resolution. The structural data confirm that the N-terminal domain of RapZ possesses a kinase fold, whereas the C-terminal domain bears closest homology to a subdomain of 6-phosphofructokinase, an important enzyme in the glycolytic pathway. RapZ self-associates into a domain swapped dimer of dimers, and in vivo data support the importance of quaternary structure in RNA-mediated regulation of target gene expression. Based on biochemical, structural and genetic data, we suggest a mechanism for binding and presentation by RapZ of GlmZ and the closely related decoy sRNA, GlmY. We discuss a scenario for the molecular evolution of RapZ through re-purpose of enzyme components from central metabolism.

PubMed: 28977623
DOI: 10.1093/nar/gkx732

実験手法

X-RAY DIFFRACTION (1.17 Å)