EC Number   |
Reference |
|---|
   7.5.2.6 | apo,MgADP/Vi-bound and MgAMP-PNP-bound MsbA, X-ray diffraction structure determination and analysis |
749889 |
| 7.5.2.6 | crystal structure analysis |
751321 |
| 7.5.2.6 | purified enzyme MsbA free and in complex with inhibitors (2E)-3-[6-[1-(2-chloro-6-cyclopropylphenyl)ethoxy]-4-cyclopropylquinolin-3-yl]prop-2-enoic acid or G902, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 50 mM Tris, pH 8.0, 500 mM NaCl, and 0.6% FA-3 detergent, with mother liquor containing 200 mM NaCl, 19% PEG 550 MME, 4% PEG 400, and 100 mM HEPES, pH 7.0, in a 1:1 v/v ratio, 19°C, 1 week, X-ray diffraction structure determination and analysis at 2.9 A resolution |
751693 |
| 7.5.2.6 | purified enzyme MsbA in complex with inhibitor G907, analysis of structure PDB ID 3B60 |
751693 |
| 7.5.2.6 | targeted molecular dynamics simulation methods reveal a clear spatiotemporal order of the conformational movements from the outward-facing to the inward-facing states. The disruption of the nucleotide binding sites at the nucleotide-binding dimer interface is the very first event that initiates the following conformational changes. The conserved x-loops of the nucleotide binding sites participate in the interaction network that stabilizes the cytoplasmic tetrahelix bundle of the transmembrane domains and play an important role in mediating the cross-talk between the nucleotide-binding domains and transmembrane domains. The movement of the nucleotide-binding domain dimer is transmitted through x-loops to break the tetrahelix bundle, inducing the packing rearrangements of the transmembrane helices at the cytoplasmic side and the periplasmic side sequentially |
719886 |
| 7.5.2.6 | X-ray diffraction structure determination and analysis at 3.7 A resolution and analysis of structure PDB ID 3b60 |
696222 |
