7AG0
 
 | | Complex between the bone morphogenetic protein 2 and its antagonist Noggin | | Descriptor: | Bone morphogenetic protein 2, GLYCEROL, Noggin | | Authors: | Robert, C, Bruck, F, Herman, R, Vandevenne, M, Filee, P, Kerff, F, Matagne, A. | | Deposit date: | 2020-09-21 | | Release date: | 2022-04-13 | | Last modified: | 2024-11-06 | | Method: | X-RAY DIFFRACTION (3.104 Å) | | Cite: | Structural analysis of the interaction between human cytokine BMP-2 and the antagonist Noggin reveals molecular details of cell chondrogenesis inhibition.
J.Biol.Chem., 299, 2023
|
|
2BH0
 | | Crystal structure of a SeMet derivative of EXPA from Bacillus subtilis at 2.5 angstrom | | Descriptor: | YOAJ | | Authors: | Petrella, S, Herman, R, Sauvage, E, Filee, P, Joris, B, Charlier, P. | | Deposit date: | 2005-01-06 | | Release date: | 2006-06-28 | | Last modified: | 2024-11-13 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Crystal Structure and Activity of Bacillus Subtilis Yoaj (Exlx1), a Bacterial Expansin that Promotes Root Colonization.
Proc.Natl.Acad.Sci.USA, 105, 2008
|
|
3D30
 | | Structure of an expansin like protein from Bacillus Subtilis at 1.9A resolution | | Descriptor: | Expansin like protein, FORMIC ACID, GLYCEROL | | Authors: | Kerff, F, Petrella, S, Herman, R, Sauvage, E, Joris, B, Charlier, P. | | Deposit date: | 2008-05-09 | | Release date: | 2008-10-14 | | Last modified: | 2023-08-30 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization.
Proc.Natl.Acad.Sci.USA, 105, 2008
|
|
1P6R
 | | Solution structure of the DNA binding domain of the repressor BlaI. | | Descriptor: | Penicillinase repressor | | Authors: | Melckebeke, H.V, Vreuls, C, Gans, P, Llabres, G, Filee, P, Joris, B, Simorre, J.P. | | Deposit date: | 2003-04-30 | | Release date: | 2003-12-09 | | Last modified: | 2024-05-22 | | Method: | SOLUTION NMR | | Cite: | Solution structural study of BlaI: implications for the repression of genes involved in beta-lactam antibiotic resistance.
J.Mol.Biol., 333, 2003
|
|
