6RPH

TR-SMX open state structure (10-15ms) of bacteriorhodopsin

Summary for 6RPH

• Entry DOI: 10.2210/pdb6rph/pdb
• Related: 6RNJ
• Descriptor: Bacteriorhodopsin, RETINAL (3 entities in total)
• Functional Keywords: retinal, time resolved crystallography, serial crystallography, smx, proton transport
• Biological source: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
• Total number of polymer chains: 1
• Total formula weight: 26538.48

Authors

Weinert, T.,Skopintsev, P.,James, D.,Kekilli, D.,Furrer, A.,Bruenle, S.,Mous, S.,Nogly, P.,Standfuss, J. (deposition date: 2019-05-14, release date: 2019-07-17, Last modification date: 2019-07-24)

Primary citation

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.
Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography.
Science, 365:61-65, 2019

PubMed Abstract: 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.

PubMed: 31273117
DOI: 10.1126/science.aaw8634

Experimental method

X-RAY DIFFRACTION (2.6 Å)