6r3t

Structure of P110 from Mycoplasma Genitalium at 2.7A

spinqualitylabelsall models 6r3t, resolution 2.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r3t is a 1 chain structure. This structure supersedes the now removed PDB entry 5mzb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: K, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors.,Aparicio D, Torres-Puig S, Ratera M, Querol E, Pinol J, Pich OQ, Fita I Nat Commun. 2018 Oct 26;9(1):4471. doi: 10.1038/s41467-018-06963-y. PMID:30367053 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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