3VE3
Structure of IT Intermediate from time-resolved laue crystallography
Summary for 3VE3
| Entry DOI | 10.2210/pdb3ve3/pdb |
| Related | 3VE4 4HY8 4I38 4I39 4I3A 4I3I 4I3J |
| Descriptor | Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (2 entities in total) |
| Functional Keywords | photoreceptor, chromophore, sensory transduction, luminescent protein |
| Biological source | Halorhodospira halophila (ECTOTHIORHODOSPIRA HALOPHILA) |
| Total number of polymer chains | 1 |
| Total formula weight | 14052.73 |
| Authors | Ihee, H.,Jung, Y.O. (deposition date: 2012-01-07, release date: 2013-03-20, Last modification date: 2025-03-26) |
| Primary citation | Jung, Y.O.,Lee, J.H.,Kim, J.,Schmidt, M.,Moffat, K.,Srajer, V.,Ihee, H. Volume-conserving trans-cis isomerization pathways in photoactive yellow protein visualized by picosecond X-ray crystallography NAT.CHEM., 5:212-220, 2013 Cited by PubMed Abstract: Trans-to-cis isomerization, the key reaction in photoactive proteins, usually cannot occur through the standard one-bond-flip mechanism. Owing to spatial constraints imposed by a protein environment, isomerization probably proceeds through a volume-conserving mechanism in which highly choreographed atomic motions are expected, the details of which have not yet been observed directly. Here we employ time-resolved X-ray crystallography to visualize structurally the isomerization of the p-coumaric acid chromophore in photoactive yellow protein with a time resolution of 100 ps and a spatial resolution of 1.6 Å. The structure of the earliest intermediate (I(T)) resembles a highly strained transition state in which the torsion angle is located halfway between the trans- and cis-isomers. The reaction trajectory of I(T) bifurcates into two structurally distinct cis intermediates via hula-twist and bicycle-pedal pathways. The bifurcating reaction pathways can be controlled by weakening the hydrogen bond between the chromophore and an adjacent residue through E46Q mutation, which switches off the bicycle-pedal pathway. PubMed: 23422563DOI: 10.1038/nchem.1565 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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