Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–3 of 3 results
Advanced filters: Author: David Vizarraga Clear advanced filters

  • M. pneumoniae, a model organism for a minimal cell, has a dedicated protein, namely P116, to specifically extract essential lipids. The structure of P116 has a previously unseen fold, resembling a left-handed baseball glove forming a huge hydrophobic cavity.

    • Lasse Sprankel
    • David Vizarraga
    • Achilleas S. Frangakis
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 321-329

  • The adhesion complex (Nap) in Mycoplasma genitalium is composed of the adhesin proteins P110 and P140 and essential for infectivity, motility and adhesion of this human pathogen. Here, the author present the structures of P140 alone and the P140/P110 complex in closed and open conformations and based on their structural data and further functional studies propose a mechanism for the attachment and release of M. genitalium to the host cell receptor.

    • David Aparicio
    • Margot P. Scheffer
    • Achilleas S. Frangakis
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • Adhesion of the human pathogen Mycoplasma pneumoniae to pulmonary epithelial cells is mediated by a transmembrane complex composed of proteins P1 and P40/P90. Here, the authors present the structures of M. pneumoniae P1 and P40/P90, show that P40/P90 binds sialylated oligosaccharides and have also determined the crystal structures of P40/P90 complexes with 3’-Sialyllactose and 6’-Sialyllactose, which provide insights into the mechanisms of adhesion and gliding on host cell surfaces.

    • David Vizarraga
    • Akihiro Kawamoto
    • David Aparicio
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-16