2XF7

Crystal structure of Bacillus subtilis SPP1 phage gp23.1, a putative chaperone. High-resolution structure.

2XF7 の概要

• エントリーDOI: 10.2210/pdb2xf7/pdb
• 関連するPDBエントリー: 2XF5 2XF6
• 分子名称: GP23.1 (2 entities in total)
• 機能のキーワード: viral protein
• 由来する生物種: BACILLUS PHAGE SPP1
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 34122.80

構造登録者

Veesler, D.,Blangy, S.,Lichiere, J.,Ortiz-Lombardia, M.,Tavares, P.,Campanacci, V.,Cambillau, C. (登録日: 2010-05-20, 公開日: 2010-08-11, 最終更新日: 2023-12-20)

主引用文献

Veesler, D.,Blangy, S.,Lichiere, J.,Ortiz-Lombardia, M.,Tavares, P.,Campanacci, V.,Cambillau, C.
Crystal Structure of Bacillus Subtilis Spp1 Phage Gp23.1, A Putative Chaperone.
Protein Sci., 19:1812-, 2010

PubMed Abstract: SPP1 is a siphophage infecting the gram-positive bacterium Bacillus subtilis. The SPP1 tail electron microscopy (EM) reconstruction revealed that it is mainly constituted by conserved structural proteins such as the major tail proteins (gp17.1), the tape measure protein (gp18), the Distal tail protein (Dit, gp19.1), and the Tail associated lysin (gp21). A group of five small genes (22-24.1) follows in the genome but it remains to be elucidated whether their protein products belong or not to the tail. Noteworthy, an unassigned EM density accounting for ~245 kDa is present at the distal end of the SPP1 tail-tip. We report here the gp23.1 crystal structure at 1.6 A resolution, a protein that lacks sequence identity to any known protein. We found that gp23.1 forms a hexamer both in the crystal lattice and in solution as revealed by light scattering measurements. The gp23.1 hexamer does not fit well in the unassigned SPP1 tail-tip EM density and we hypothesize that this protein might act as a chaperone.

PubMed: 20665904
DOI: 10.1002/PRO.464

実験手法

X-RAY DIFFRACTION (1.61 Å)