7DZI

intermediate of FABP with a delay time of 300 ns

Summary for 7DZI

• Entry DOI: 10.2210/pdb7dzi/pdb
• Descriptor: Fatty acid-binding protein, liver, PALMITIC ACID (3 entities in total)
• Functional Keywords: fabp, recombination
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 31784.51

Authors

Li, H.,Yu, L.-J.,Liu, X.,Shen, J.-R.,Wang, J. (deposition date: 2021-01-25, release date: 2022-07-27, Last modification date: 2023-11-29)

Primary citation

Liu, X.,Liu, P.,Li, H.,Xu, Z.,Jia, L.,Xia, Y.,Yu, M.,Tang, W.,Zhu, X.,Chen, C.,Zhang, Y.,Nango, E.,Tanaka, R.,Luo, F.,Kato, K.,Nakajima, Y.,Kishi, S.,Yu, H.,Matsubara, N.,Owada, S.,Tono, K.,Iwata, S.,Yu, L.J.,Shen, J.R.,Wang, J.
Excited-state intermediates in a designer protein encoding a phototrigger caught by an X-ray free-electron laser.
Nat.Chem., 14:1054-1060, 2022

PubMed Abstract: One of the primary objectives in chemistry research is to observe atomic motions during reactions in real time. Although X-ray free-electron lasers (XFELs) have facilitated the capture of reaction intermediates using time-resolved serial femtosecond crystallography (TR-SFX), only a few natural photoactive proteins have been investigated using this method, mostly due to the lack of suitable phototriggers. Here we report the genetic encoding of a xanthone amino acid (FXO), as an efficient phototrigger, into a rationally designed human liver fatty-acid binding protein mutant (termed XOM), which undergoes photo-induced C-H bond transformation with high selectivity and quantum efficiency. We solved the structures of XOM before and 10-300 ns after flash illumination, at 1.55-1.70 Å resolutions, and captured the elusive excited-state intermediates responsible for precise C-H bond activation. We expect that most redox enzymes can now be investigated by TR-SFX, using our method, to reveal reaction intermediates key for their efficiency and selectivity.

PubMed: 35851837
DOI: 10.1038/s41557-022-00992-3

Experimental method

X-RAY DIFFRACTION (1.65 Å)