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- Complex Structure and Biochemical Characterization of the . . .
The Staphylococcus aureus PII-like signal transduction protein PstA was recently identified as a cyclic diadenylate monophosphate (c-di-AMP)-binding protein Here, we present the crystal structures of the apo- and c-di-AMP-bound PstA protein, which is trimeric in solution as well as in the crystals
- Crystal structure of Listeria monocytogenes PstA in complex with . . .
Download scientific diagram | Crystal structure of Listeria monocytogenes PstA in complex with cyclic-di-AMP (c-di-AMP)
- pstA - Phosphate transport system permease protein PstA - Escherichia . . .
Belongs to the binding-protein-dependent transport system permease family CysTW subfamily View the Phylogenomic databases for this entry within the Similar Proteins section View all family and domain features for this entry's canonical sequence in the UniParc Feature Viewer Search…
- Free P Sta+Durchgesiebt Photos - Pexels
Download and use 3,000+ Psta+durchgesiebt stock photos for free Thousands of new images every day Completely Free to Use High-quality videos and images from Pexels
- PSTA - Pinellas Suncoast Transit Authority – Public Transit in . . .
Plan your trip, explore routes, and stay connected with PSTA: your public transit system serving St Petersburg and Pinellas County
- Psta Durchgesiebt Stock Photos - Dreamstime
Search among 48 authentic psta stock photos, high-definition images, and pictures, or look at other food or healthy stock images to enhance your presentation with the perfect visual
- c-di-AMP recognition by Staphylococcus aureus PstA
We solved the crystal structures of S aureus PstA with and without its ligand c-di-AMP and were thus able to analyze the coordination of c-di-AMP and subsequent structural changes in PstA
- Molecular basis for the recognition of cyclic-di-AMP by PstA, a PII . . .
PstA forms a homotrimer structure that has overall similarity to the PII protein family which binds ATP However, PstA is markedly different from PII proteins in the loop regions, and these structural differences mediate the specific recognition of their respective nucleotide ligand
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