7CRX
Structure of Chloride ion pumping rhodopsin (ClR) with NTQ motif 100 ps after light activation (2.63mJ/mm2)
Summary for 7CRX
Entry DOI | 10.2210/pdb7crx/pdb |
Descriptor | Chloride pumping rhodopsin, CHLORIDE ION, RETINAL, ... (5 entities in total) |
Functional Keywords | chloride ion pumping rhodopsin, sfx, xfel, clr, ntq, membrane protein |
Biological source | Nonlabens marinus S1-08 |
Total number of polymer chains | 1 |
Total formula weight | 31731.09 |
Authors | Yun, J.H.,Liu, H.,Lee, W.T.,Schmidt, M. (deposition date: 2020-08-14, release date: 2021-04-14, Last modification date: 2023-11-29) |
Primary citation | Yun, J.H.,Li, X.,Yue, J.,Park, J.H.,Jin, Z.,Li, C.,Hu, H.,Shi, Y.,Pandey, S.,Carbajo, S.,Boutet, S.,Hunter, M.S.,Liang, M.,Sierra, R.G.,Lane, T.J.,Zhou, L.,Weierstall, U.,Zatsepin, N.A.,Ohki, M.,Tame, J.R.H.,Park, S.Y.,Spence, J.C.H.,Zhang, W.,Schmidt, M.,Lee, W.,Liu, H. Early-stage dynamics of chloride ion-pumping rhodopsin revealed by a femtosecond X-ray laser. Proc.Natl.Acad.Sci.USA, 118:-, 2021 Cited by PubMed Abstract: Chloride ion-pumping rhodopsin (ClR) in some marine bacteria utilizes light energy to actively transport Cl into cells. How the ClR initiates the transport is elusive. Here, we show the dynamics of ion transport observed with time-resolved serial femtosecond (fs) crystallography using the Linac Coherent Light Source. X-ray pulses captured structural changes in ClR upon flash illumination with a 550 nm fs-pumping laser. High-resolution structures for five time points (dark to 100 ps after flashing) reveal complex and coordinated dynamics comprising retinal isomerization, water molecule rearrangement, and conformational changes of various residues. Combining data from time-resolved spectroscopy experiments and molecular dynamics simulations, this study reveals that the chloride ion close to the Schiff base undergoes a dissociation-diffusion process upon light-triggered retinal isomerization. PubMed: 33753488DOI: 10.1073/pnas.2020486118 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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