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7CRL

Structure of Chloride ion pumping rhodopsin (ClR) with NTQ motif 50 ps after light activation

Summary for 7CRL
Entry DOI10.2210/pdb7crl/pdb
DescriptorChloride pumping rhodopsin, CHLORIDE ION, RETINAL, ... (5 entities in total)
Functional Keywordschloride ion pumping rhodopsin, sfx, xfel, clr, ntq, membrane protein
Biological sourceNonlabens marinus S1-08
Total number of polymer chains1
Total formula weight31731.09
Authors
Yun, J.H.,Liu, H.,Lee, W.T.,Schmidt, M. (deposition date: 2020-08-13, release date: 2021-04-14, Last modification date: 2024-10-23)
Primary citationYun, 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: 33753488
DOI: 10.1073/pnas.2020486118
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

226707

数据于2024-10-30公开中

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