7AGZ
BsrV no-histagged
Summary for 7AGZ
| Entry DOI | 10.2210/pdb7agz/pdb |
| Descriptor | Broad specificity amino-acid racemase, PYRIDOXAL-5'-PHOSPHATE, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | broad spectrum, racemase, peptidoglycan binding protein, peptide binding protein |
| Biological source | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
| Total number of polymer chains | 2 |
| Total formula weight | 85777.50 |
| Authors | Carrasco-Lopez, C.,Rojas-Altuve, A.,Espaillat, A.,Cava, F.,Hermoso, J.A. (deposition date: 2020-09-23, release date: 2021-10-06, Last modification date: 2024-01-31) |
| Primary citation | Espaillat, A.,Carrasco-Lopez, C.,Bernardo-Garcia, N.,Rojas-Altuve, A.,Klett, J.,Morreale, A.,Hermoso, J.A.,Cava, F. Binding of non-canonical peptidoglycan controls Vibrio cholerae broad spectrum racemase activity. Comput Struct Biotechnol J, 19:1119-1126, 2021 Cited by PubMed Abstract: Broad-spectrum amino acid racemases (Bsrs) enable bacteria to generate non-canonical D-amino acids (NCDAAs), whose roles and impact on microbial physiology, including modulation of cell wall structure and dissolution of biofilms, are just beginning to be appreciated. Here we used a diverse array of structural, biochemical and molecular simulation studies to define and characterize how BsrV is post-translationally regulated. We discovered that contrary to alanine racemase AlrV highly compacted active site, BsrV's is broader and can be occupied by cell wall stem peptides. We found that peptidoglycan peptides modified with NCDAAs are better stabilized by BsrV's catalytic cavity and show better inhibitory capacity than canonical muropeptides. Notably, BsrV binding and inhibition can be recapitulated by undigested peptidoglycan sacculi as it exists in the cell. Docking simulations of BsrV binding the peptidoglycan polymer generate a model where the peptide stems are perfectly accommodated and stabilized within each of the dimeŕs active sites. Taking these biochemical and structural data together, we propose that inhibition of BsrV by peptidoglycan peptides underlies a negative regulatory mechanism to avoid excessive NCDAA production. Our results collectively open the door to use "à la carte" synthetic peptides as a tool to modulate DAAs production of Bsr enzymes. PubMed: 33680355DOI: 10.1016/j.csbj.2021.01.031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.52 Å) |
Structure validation
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