Protein interactions involving intrinsically disordered proteins (IDPs) comprise a variety of binding modes, from the well-characterized folding upon binding to dynamic fuzzy complexes. To date, most studies concern the binding of an IDP to a structured protein, while the interaction between two IDPs is poorly understood. In this study, NMR, smFRET, and molecular dynamics (MD) simulation are combined to characterize the interaction between two IDPs, the C-terminal domain (CTD) of protein 4.1G and the nuclear mitotic apparatus (NuMA) protein. It is revealed that CTD and NuMA form a fuzzy complex with remaining structural disorder. Multiple binding sites on both proteins were identified by molecular dynamics and mutagenesis studies. This study provides an atomic scenario in which two IDPs bearing multiple binding sites interact with each other in dynamic equilibrium. The combined approach employed here could be widely applicable for investigating IDPs and their dynamic interactions.
The glutamine binding protein (GlnBP) binds l-glutamine and cooperates with its cognate transporters during glutamine uptake. Crystal structure analysis has revealed an open and a closed conformation for apo- and holo-GlnBP, respectively. However, the detailed conformational dynamics have remained unclear. Herein, we combined NMR spectroscopy, MD simulations, and single-molecule FRET techniques to decipher the conformational dynamics of apo-GlnBP. The NMR residual dipolar couplings of apo-GlnBP were in good agreement with a MD-derived structure ensemble consisting of four metastable states. The open and closed conformations are the two major states. This four-state model was further validated by smFRET experiments and suggests the conformational selection mechanism in ligand recognition of GlnBP.
Protein dynamics plays key roles in ligand binding. However, the microscopic description of conformational dynamics-coupled ligand binding remains a challenge. In this study, we integrate molecular dynamics simulations, Markov state model (MSM) analysis and experimental methods to characterize the conformational dynamics of ligand-bound glutamine binding protein (GlnBP). We show that ligand-bound GlnBP has high conformational flexibility and additional metastable binding sites, presenting a more complex energy landscape than the scenario in the absence of ligand. The diverse conformations of GlnBP demonstrate different binding affinities and entail complex transition kinetics, implicating a concerted ligand binding mechanism. Single molecule fluorescence resonance energy transfer measurements and mutagenesis experiments are performed to validate our MSM-derived structure ensemble as well as the binding mechanism. Collectively, our study provides deeper insights into the protein dynamics-coupled ligand binding, revealing an intricate regulatory network underlying the apparent binding affinity.
Parasitoidism is a key innovation in insect evolution, and parasitoid insects, nowadays, play a significant role in structuring ecological communities. Despite their diversity and ecological impact, little is known about the early evolution and ecology of parasitoid insects, especially parasitoid true flies (Diptera). Here, we describe a bizarre fly, Zhenia xiai gen. et sp. nov., from Late Cretaceous Burmese amber (about 99 million years old) that represents the latest occurrence of the family Eremochaetidae. Z. xiai is an endoparasitoid insect as evidenced by a highly developed, hypodermic-like ovipositor formed by abdominal tergites VIII + IX that was used for injecting eggs into hosts and enlarged tridactylous claws supposedly for clasping hosts. Our results suggest that eremochaetids are among the earliest definite records of parasitoid insects. Our findings reveal an unexpected morphological specialization of flies and broaden our understanding of the evolution and diversity of ancient parasitoid insects.
The glutamine binding protein (GlnBP) binds l‐glutamine and cooperates with its cognate transporters during glutamine uptake. Crystal structure analysis has revealed an open and a closed conformation for apo‐ and holo‐GlnBP, respectively. However, the detailed conformational dynamics have remained unclear. Herein, we combined NMR spectroscopy, MD simulations, and single‐molecule FRET techniques to decipher the conformational dynamics of apo‐GlnBP. The NMR residual dipolar couplings of apo‐GlnBP were in good agreement with a MD‐derived structure ensemble consisting of four metastable states. The open and closed conformations are the two major states. This four‐state model was further validated by smFRET experiments and suggests the conformational selection mechanism in ligand recognition of GlnBP.
Large-scale single-crystal cubic PbS nanorods were successfully achieved by using ultrasound irradiation in certain ethylenediamine tetraacetic acid (EDTA) solutions, particularly in the solution of Pb:EDTA = 1:1. The obtained PbS nanorods were characterized using x-ray diffraction, scanning electron microscopy, transmission electron microscopy, energy-dispersed x-ray spectrometry, selected area electronic diffraction, and high-resolution transmission electron microscopy. The results reveal that the PbS nanorods with straight and uniform structure have a diameter of about 70–80 nm and length of about 1000 nm, where the growth mechanism is tentatively discussed. The successful synthesis of these cubic structure semiconductor PbS nanorods may open up new possibilities for using these materials as building blocks to create functional two-dimensional or three-dimensional nanostructured materials.
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