6DGM
Streptococcus pyogenes phosphoglycerol transferase GacH in complex with sn-glycerol-1-phosphate
Summary for 6DGM
| Entry DOI | 10.2210/pdb6dgm/pdb |
| Related | 5U9Z |
| Descriptor | Phosphoglycerol transferase GacH, MANGANESE (II) ION, SN-GLYCEROL-1-PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | group a streptococcus (gas), lancefield group a carbohydrate, glycero-1-phosphate, l-glycerol 1-phosphate, d-glycerol-3-phosphate, transferase |
| Biological source | Streptococcus pyogenes MGAS5005 |
| Total number of polymer chains | 2 |
| Total formula weight | 87030.87 |
| Authors | Edgar, R.J.,Korotkova, N.,Korotkov, K.V. (deposition date: 2018-05-17, release date: 2018-06-06, Last modification date: 2023-10-11) |
| Primary citation | Edgar, R.J.,van Hensbergen, V.P.,Ruda, A.,Turner, A.G.,Deng, P.,Le Breton, Y.,El-Sayed, N.M.,Belew, A.T.,McIver, K.S.,McEwan, A.G.,Morris, A.J.,Lambeau, G.,Walker, M.J.,Rush, J.S.,Korotkov, K.V.,Widmalm, G.,van Sorge, N.M.,Korotkova, N. Discovery of glycerol phosphate modification on streptococcal rhamnose polysaccharides. Nat.Chem.Biol., 15:463-471, 2019 Cited by PubMed Abstract: Cell wall glycopolymers on the surface of Gram-positive bacteria are fundamental to bacterial physiology and infection biology. Here we identify gacH, a gene in the Streptococcus pyogenes group A carbohydrate (GAC) biosynthetic cluster, in two independent transposon library screens for its ability to confer resistance to zinc and susceptibility to the bactericidal enzyme human group IIA-secreted phospholipase A. Subsequent structural and phylogenetic analysis of the GacH extracellular domain revealed that GacH represents an alternative class of glycerol phosphate transferase. We detected the presence of glycerol phosphate in the GAC, as well as the serotype c carbohydrate from Streptococcus mutans, which depended on the presence of the respective gacH homologs. Finally, nuclear magnetic resonance analysis of GAC confirmed that glycerol phosphate is attached to approximately 25% of the GAC N-acetylglucosamine side-chains at the C6 hydroxyl group. This previously unrecognized structural modification impacts host-pathogen interaction and has implications for vaccine design. PubMed: 30936502DOI: 10.1038/s41589-019-0251-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.49 Å) |
Structure validation
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