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X-ray Structure and Ligand Binding Study of a Moth Chemosensory Protein*
TLDR
Fluorescence quenching with brominated alkyl alcohols or fatty acids and modeling studies indicates that CSPMbraA6 is able to bind such compounds with C12–18 alkyL chains.
Deciphering the Xcp Pseudomonas aeruginosa Type II Secretion Machinery through Multiple Interactions with Substrates*♦
TLDR
A model of the different consecutive steps followed by the substrate during the type II secretion process is proposed, which validates the piston model hypothesis, in which the pseudopilus pushes the substrate through the secretin pore during the secretion process.
Revisiting the Specificity of Mamestra brassicaeand Antheraea polyphemus Pheromone-binding Proteins with a Fluorescence Binding Assay*
TLDR
Investigation of the binding properties and specificity of PBPs from Mamestra brassicae, Antheraea polyphemus, Bombyx mori, and a hexa-mutant of MbraPBP1, indicates that relatively limited modifications to the PBP cavity actually interfere with AMA binding, suggesting that AMA binds in the internal cavity.
The XcpV/GspI Pseudopilin Has a Central Role in the Assembly of a Quaternary Complex within the T2SS Pseudopilus*
TLDR
Two biochemical techniques are combined to investigate the protein-protein interaction network between the five Pseudomonas aeruginosa Xcp pseudopilins and suggest the existence of a quaternary, rather than ternary, complex at the tip of the pseudopilus.
Mammalian odorant binding proteins.
The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism.
TLDR
Comparisons with other OBPs indicate that the two cysteines involved in the O BPp disulfide bridge are conserved in the sequence, suggesting that OBPp may be considered a prototypic OBP fold, and not OBPb.
The Crystal Structure of a Cockroach Pheromone-binding Protein Suggests a New Ligand Binding and Release Mechanism*
TLDR
Differences between LmaPBP and BmorPBP structures suggest that different binding and release mechanism may be adapted to the hydrophilicity or hydrophobicity of the pheromonal ligand.
Moth chemosensory protein exhibits drastic conformational changes and cooperativity on ligand binding
TLDR
The x-ray structure of CSPMbraA6, a 112-aa antennal protein from the moth Mamestra brassicae (Mbra), was shown to exhibit a novel type of α-helical fold and binding cooperativity was demonstrated for some ligands, suggesting a stepwise binding.
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