1S1Z
Photoactivated chromophore conformation in Photoactive Yellow Protein (E46Q mutant) from 10 to 500 nanoseconds
Summary for 1S1Z
Entry DOI | 10.2210/pdb1s1z/pdb |
Related | 1S1Y |
Descriptor | Photoactive Yellow Protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total) |
Functional Keywords | room temperature, time-resolved, photoreceptor |
Biological source | Halorhodospira halophila |
Total number of polymer chains | 1 |
Total formula weight | 14051.75 |
Authors | Anderson, S.,Srajer, V.,Pahl, R.,Rajagopal, S.,Schotte, F.,Anfinrud, P.,Wulff, M.,Moffat, K. (deposition date: 2004-01-07, release date: 2004-06-15, Last modification date: 2021-10-27) |
Primary citation | Anderson, S.,Srajer, V.,Pahl, R.,Rajagopal, S.,Schotte, F.,Anfinrud, P.,Wulff, M.,Moffat, K. Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein Structure, 12:1039-1045, 2004 Cited by PubMed Abstract: We use time-resolved crystallography to observe the structural progression of a bacterial blue light photoreceptor throughout its photocycle. Data were collected from 10 ns to 100 ms after photoactivation of the E46Q mutant of photoactive yellow protein. Refinement of transient chromophore conformations shows that the spectroscopically distinct intermediates are formed via progressive disruption of the hydrogen bond network to the chromophore. Although structural change occurs within a few nanoseconds on and around the chromophore, it takes milliseconds for a distinct pattern of tertiary structural change to fully progress through the entire molecule, thus generating the putative signaling state. Remarkably, the coupling between the chromophore conformation and the tertiary structure of this small protein is not tight: there are leads and lags between changes in the conformation of the chromophore and the protein tertiary structure. PubMed: 15274923DOI: 10.1016/j.str.2004.04.008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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