2BH0

Crystal structure of a SeMet derivative of EXPA from Bacillus subtilis at 2.5 angstrom

2BH0 の概要

• エントリーDOI: 10.2210/pdb2bh0/pdb
• 分子名称: YOAJ (2 entities in total)
• 機能のキーワード: cell adhesion, expansin related protein, bacillus subtilis, expansins
• 由来する生物種: BACILLUS SUBTILIS
• 細胞内の位置: Secreted, cell wall: O34918
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23471.48

構造登録者

Petrella, S.,Herman, R.,Sauvage, E.,Filee, P.,Joris, B.,Charlier, P. (登録日: 2005-01-06, 公開日: 2006-06-28, 最終更新日: 2024-11-13)

主引用文献

Kerff, F.,Amoroso, A.,Herman, R.,Sauvage, E.,Petrella, S.,Fileee, P.,Charlier, P.,Joris, B.,Tabuchi, A.,Nikolaidis, N.,Cosgrove, D.J.
Crystal Structure and Activity of Bacillus Subtilis Yoaj (Exlx1), a Bacterial Expansin that Promotes Root Colonization.
Proc.Natl.Acad.Sci.USA, 105:16876-, 2008

PubMed Abstract: We solved the crystal structure of a secreted protein, EXLX1, encoded by the yoaJ gene of Bacillus subtilis. Its structure is remarkably similar to that of plant beta-expansins (group 1 grass pollen allergens), consisting of 2 tightly packed domains (D1, D2) with a potential polysaccharide-binding surface spanning the 2 domains. Domain D1 has a double-psi beta-barrel fold with partial conservation of the catalytic site found in family 45 glycosyl hydrolases and in the MltA family of lytic transglycosylases. Domain D2 has an Ig-like fold similar to group 2/3 grass pollen allergens, with structural features similar to a type A carbohydrate-binding domain. EXLX1 bound to plant cell walls, cellulose, and peptidoglycan, but it lacked lytic activity against a variety of plant cell wall polysaccharides and peptidoglycan. EXLX1 promoted plant cell wall extension similar to, but 10 times weaker than, plant beta-expansins, which synergistically enhanced EXLX1 activity. Deletion of the gene encoding EXLX1 did not affect growth or peptidoglycan composition of B. subtilis in liquid medium, but slowed lysis upon osmotic shock and greatly reduced the ability of the bacterium to colonize maize roots. The presence of EXLX1 homologs in a small but diverse set of plant pathogens further supports a role in plant-bacterial interactions. Because plant expansins have proved difficult to express in active form in heterologous systems, the discovery of a bacterial homolog opens the door for detailed structural studies of expansin function.

PubMed: 18971341
DOI: 10.1073/PNAS.0809382105

実験手法

X-RAY DIFFRACTION (2.5 Å)