Summary for 6R43
| Entry DOI | 10.2210/pdb6r43/pdb |
| Related | 6R3T 6R41 |
| Related PRD ID | PRD_900066 |
| Descriptor | Mgp-operon protein 3, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | adhesin, sugar binding protein |
| Biological source | Mycoplasma genitalium G37 |
| Total number of polymer chains | 1 |
| Total formula weight | 100322.82 |
| Authors | Aparicio, D.,Fita, I. (deposition date: 2019-03-21, release date: 2019-04-10, Last modification date: 2024-01-24) |
| Primary citation | Aparicio, D.,Torres-Puig, S.,Ratera, M.,Querol, E.,Pinol, J.,Pich, O.Q.,Fita, I. Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors. Nat Commun, 9:4471-4471, 2018 Cited by PubMed Abstract: Adhesion of pathogenic bacteria to target cells is a prerequisite for colonization and further infection. The main adhesins of the emerging sexually transmitted pathogen Mycoplasma genitalium, P140 and P110, interact to form a Nap complex anchored to the cell membrane. Herein, we present the crystal structures of the extracellular region of the virulence factor P110 (916 residues) unliganded and in complex with sialic acid oligosaccharides. P110 interacts only with the neuraminic acid moiety of the oligosaccharides and experiments with human cells demonstrate that these interactions are essential for mycoplasma cytadherence. Additionally, structural information provides a deep insight of the P110 antigenic regions undergoing programmed variation to evade the host immune response. These results enlighten the interplay of M. genitalium with human target cells, offering new strategies to control mycoplasma infections. PubMed: 30367053DOI: 10.1038/s41467-018-06963-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.52 Å) |
Structure validation
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