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DTSTAMP:20220718T082336Z
DTSTART:20220706T170000
DTEND:20220706T180000
SUMMARY:UniSysCat - Colloquium
DESCRIPTION:Time-resolved X-ray crystallography on membrane proteins: Watching ions moving in time and space\nDr. Przemyslaw Nogly\nETH Zürich and soon at the Jagiellonian University, Krakow\nChloride transport is an essential process maintaining ion balance across cell membranes, cell growth and neuronal action potentials, however, the molecular mechanism of the transport remains elusive. Among chloride transporters, light-driven rhodopsins have gained attention as optogenetic tools to manipulate neuronal signalling. Ion pumping microbial rhodopsins are integral membrane proteins employing a common 7-transmembrane helices architecture to transport different ion types. The specific residue composition impacts the protein dynamics, transport mechanism and ion selectivity.\nWe combined time-resolved serial crystallography (SwissFEL and SLS synchrotron) to provide a comprehensive view of the structural dynamics and molecular mechanism of a chloride pumping rhodopsin throughout the transport cycle from 10 ps to 50 ms [1]. We traced transient anion binding sites, obtained evidence for the mechanism of light energy utilization in transport and identified steric and electrostatic molecular gates ensuring unidirectional transport. These structural insights unravel the key mechanistic features enabling finely controlled chloride transport across the cell membrane.\n[1] Mous, S. et al. Science 2022, 375, 845-851\n\n\n
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