1KOU: Crystal Structure Of The Photoactive Yellow Protein Reconstituted With Caffeic Acid At 1.16 A Resolution

A structural study is described of the photoactive yellow protein (PYP) reconstituted with the chromophore derivative 3,4-dihydroxycinnamic acid. The crystal structure of PYP reconstituted with this chromophore at 1.16 A resolution is reported in space group P6(5). This is the first high-resolution structure of a photoreceptor containing a modified chromophore. The introduction of an extra hydroxyl group in the native chromophore (i.e. p-coumaric acid) appears to perturb the structure of the hybrid yellow protein only slightly. The chromophore is bound by the protein in two different conformations, separated by a rotation of 180 degrees of the catechol ring. In combination with available spectroscopic data, it is concluded that the caffeic acid chromophore binds to the protein in a strained conformation, which leads to a faster ejection from the chromophore-binding pocket upon pB formation.
PDB ID: 1KOUDownload
MMDB ID: 71204
PDB Deposition Date: 2001/12/22
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.16  Å
Source Organism:
Similar Structures:
Biological Unit for 1KOU: monomeric; determined by author
Molecular Components in 1KOU
Label Count Molecule
Protein (1 molecule)
Photoactive Yellow Protein
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB