6rqp

Steady-state-SMX dark state structure of bacteriorhodopsin

spinqualitylabelsall models 6rqp, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rqp is a 1 chain structure with sequence from Halobacterium salinarum NRC-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: LI1, OLC, RET Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BACR_HALSA Light-driven proton pump. Publication Abstract from PubMed Conformational dynamics are essential for proteins to function. We adapted time-resolved serial crystallography developed at x-ray lasers to visualize protein motions using synchrotrons. We recorded the structural changes in the light-driven proton-pump bacteriorhodopsin over 200 milliseconds in time. The snapshot from the first 5 milliseconds after photoactivation shows structural changes associated with proton release at a quality comparable to that of previous x-ray laser experiments. From 10 to 15 milliseconds onwards, we observe large additional structural rearrangements up to 9 angstroms on the cytoplasmic side. Rotation of leucine-93 and phenylalanine-219 opens a hydrophobic barrier, leading to the formation of a water chain connecting the intracellular aspartic acid-96 with the retinal Schiff base. The formation of this proton wire recharges the membrane pump with a proton for the next cycle. Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography.,Weinert T, Skopintsev P, James D, Dworkowski F, Panepucci E, Kekilli D, Furrer A, Brunle S, Mous S, Ozerov D, Nogly P, Wang M, Standfuss J Science. 2019 Jul 5;365(6448):61-65. doi: 10.1126/science.aaw8634. PMID:31273117 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bacteriorhodopsin 3D structures

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