1KOU

Crystal Structure of the Photoactive Yellow Protein Reconstituted with Caffeic Acid at 1.16 A Resolution

Summary for 1KOU

• Entry DOI: 10.2210/pdb1kou/pdb
• Related: 1D7E
• Descriptor: PHOTOACTIVE YELLOW PROTEIN, CAFFEIC ACID, N-BUTANE, ... (4 entities in total)
• Functional Keywords: photoreceptor, photosynthesis
• Biological source: Halorhodospira halophila
• Total number of polymer chains: 1
• Total formula weight: 14126.85

Authors

van Aalten, D.M.F.,Crielaard, W.,Hellingwerf, K.J.,Joshua-Tor, L. (deposition date: 2001-12-22, release date: 2002-04-03, Last modification date: 2024-11-13)

Primary citation

van Aalten, D.M.,Crielaard, W.,Hellingwerf, K.J.,Joshua-Tor, L.
Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 A resolution.
Acta Crystallogr.,Sect.D, 58:585-590, 2002

PubMed Abstract: 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.

PubMed: 11914481
DOI: 10.1107/S0907444902001257

Experimental method

X-RAY DIFFRACTION (1.16 Å)