Reference : Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansi...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/23499
Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization.
English
Kerff, Frédéric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Amoroso, Ana Maria mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Herman, Raphaël mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Sauvage, Eric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Petrella, Stephanie [> > > >]
Filée, Patrice [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Charlier, Paulette mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Joris, Bernard mailto [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes - Centre d'ingénierie des protéines >]
Tabuchi, Akira [> > > >]
Nikolaidis, Nikolas [> > > >]
Cosgrove, Daniel J [> > > >]
2008
Proceedings of the National Academy of Sciences of the United States of America
National Academy of Sciences
105
44
16876-81
Yes (verified by ORBi)
International
0027-8424
1091-6490
Washington
DC
[en] Amino Acid Motifs ; Amino Acid Sequence ; Bacillus subtilis/metabolism ; Bacterial Proteins/chemistry ; Cell Wall/metabolism ; Crystallography, X-Ray ; Genes, Bacterial ; Models, Molecular ; Molecular Sequence Data ; Plant Roots/microbiology ; Protein Structure, Secondary ; Sequence Alignment ; Zea mays/metabolism
[en] 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.
http://hdl.handle.net/2268/23499
10.1073/pnas.0809382105

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