3OEO

The crystal structure E. coli Spy

3OEO の概要

• エントリーDOI: 10.2210/pdb3oeo/pdb
• 関連するPDBエントリー: 3OEJ
• 分子名称: Spheroplast protein Y, CADMIUM ION (3 entities in total)
• 機能のキーワード: ltxxq, extracytoplasmic stress response-related, signaling protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66218.56

構造登録者

Kwon, E.,Kim, D.Y.,Gross, C.A.,Gross, J.D.,Kim, K.K. (登録日: 2010-08-13, 公開日: 2010-09-22, 最終更新日: 2024-02-21)

主引用文献

Kwon, E.,Kim, D.Y.,Gross, C.A.,Gross, J.D.,Kim, K.K.
The crystal structure Escherichia coli Spy.
Protein Sci., 19:2252-2259, 2010

PubMed Abstract: Escherichia coli spheroplast protein y (EcSpy) is a small periplasmic protein that is homologous with CpxP, an inhibitor of the extracytoplasmic stress response. Stress conditions such as spheroplast formation induce the expression of Spy via the Cpx or the Bae two-component systems in E. coli, though the function of Spy is unknown. Here, we report the crystal structure of EcSpy, which reveals a long kinked hairpin-like structure of four α-helices that form an antiparallel dimer. The dimer contains a curved oval shape with a highly positively charged concave surface that may function as a ligand binding site. Sequence analysis reveals that Spy is highly conserved over the Enterobacteriaceae family. Notably, three conserved regions that contain identical residues and two LTxxQ motifs are placed at the horizontal end of the dimer structure, stabilizing the overall fold. CpxP also contains the conserved sequence motifs and has a predicted secondary structure similar to Spy, suggesting that Spy and CpxP likely share the same fold.

PubMed: 20799348
DOI: 10.1002/pro.489

実験手法

X-RAY DIFFRACTION (2.7 Å)