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Molecular basis of substrate-induced permeation by an amino acid antiporter
Transporters of the amino acid, polyamine and organocation (APC) superfamily play essential roles in cell redox balance, cancer, and aminoacidurias. The bacterial L-arginine/agmatine antiporter,
Substrate Binding Tunes Conformational Flexibility and Kinetic Stability of an Amino Acid Antiporter*
TLDR
The unbound state of SteT shows a reduced conformational flexibility to facilitate specific substrate binding and a reduced kinetic stability to enable rapid switching to the bound state, which supports the working model of antiporters in which alternate substrate access from one to the other membrane surface occurs in the substrate-bound state.
High-throughput single-molecule force spectroscopy for membrane proteins.
TLDR
A semi-automated high-throughput SMFS (HT-SMFS) procedure for efficient data acquisition and a coarse filter to efficiently extract protein unfolding events from large data sets are developed.
Functional and Structural Characterization of the First Prokaryotic Member of the L-Amino Acid Transporter (LAT) Family
TLDR
To the authors' knowledge, this is the first functional characterization of a prokaryotic member of the LAT family and the first structural data on an APC (amino acids, polyamines, and choline for organocations) transporter.
Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors
TLDR
The crystal structures of the extracellular region of the virulence factor P110 unliganded and in complex with sialic acid oligosaccharides are presented and identified as the P110 domain that binds to sialylated receptors essential for mycoplasma cytadherence.
Role of Transmembrane Domain 8 in Substrate Selectivity and Translocation of SteT, a Member of the l-Amino Acid Transporter (LAT) Family*
TLDR
It is suggested that TM8 sculpts the substrate-binding site and undergoes conformational changes during the transport cycle of SteT, and Lys-295 is a main determinant in the recognition of the side chain of Ste T substrates.
Projection Structure of a Member of the Amino Acid/Polyamine/Organocation Transporter Superfamily*
TLDR
Two-dimensional crystals of AdiC-W293L yielded the first detailed view of a transport protein from the APC superfamily at sub-nanometer resolution.
A Major Determinant for Gliding Motility in Mycoplasma genitalium
TLDR
The interaction between MG200 and MG491, two of the main components of the TO wheel complex that connects the TO with the cell body and the cell membrane, is described, indicating that the MG200-MG491 interaction plays a key role in the stability and functioning of the To.
Structural characterization of the NAP; the major adhesion complex of the human pathogen Mycoplasma genitalium
TLDR
Cryo‐electron tomography of intact cells and detergent permeabilized M. genitalium cell aggregates provides sub‐tomogram averages of free and cell‐attached NAPs respectively, revealing a tetrameric complex with two‐fold rotational (C2) symmetry.
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium
TLDR
The author presents 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.
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