6YRK
P140-P110 complex fitted into the cryo-electron density map of the heterodimer
Summary for 6YRK
| Entry DOI | 10.2210/pdb6yrk/pdb |
| Related | 6RUT 6S3U |
| EMDB information | 10259 10260 10890 |
| Descriptor | Mgp-operon protein 3, Adhesin P1 (2 entities in total) |
| Functional Keywords | p110/p140 nap mycoplasma genitalium surface adhesin, cell adhesion |
| Biological source | Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) More |
| Total number of polymer chains | 2 |
| Total formula weight | 213264.62 |
| Authors | Scheffer, M.P.,Aparicio, D. (deposition date: 2020-04-20, release date: 2020-06-24, Last modification date: 2024-05-22) |
| Primary citation | Aparicio, D.,Scheffer, M.P.,Marcos-Silva, M.,Vizarraga, D.,Sprankel, L.,Ratera, M.,Weber, M.S.,Seybert, A.,Torres-Puig, S.,Gonzalez-Gonzalez, L.,Reitz, J.,Querol, E.,Pinol, J.,Pich, O.Q.,Fita, I.,Frangakis, A.S. Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium. Nat Commun, 11:2877-2877, 2020 Cited by PubMed Abstract: Mycoplasma genitalium is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. Here we report the crystal structure of P140 both alone and in complex with the N-terminal domain of P110. By cryo-electron microscopy (cryo-EM) and tomography (cryo-ET) we find closed and open Nap conformations, determined at 9.8 and 15 Å, respectively. Both crystal structures and the cryo-EM structure are found in a closed conformation, where the sialic acid binding site in P110 is occluded. By contrast, the cryo-ET structure shows an open conformation, where the binding site is accessible. Structural information, in combination with functional studies, suggests a mechanism for attachment and release of M. genitalium to and from the host cell receptor, in which Nap conformations alternate to sustain motility and guarantee infectivity. PubMed: 32513917DOI: 10.1038/s41467-020-16511-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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