Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 Å resolution

Van Aalten, D. M. F., Crielaard, W., Hellingwerf, K. J., Joshua-Tor, L. (2002) Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 Å resolution. Acta Crystallographica Section D: Biological Crystallography, 58 (4). pp. 585-590. ISSN 09074449 (ISSN) (Public Dataset)

DOI: 10.1107/s0907444902001257


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 Å resolution is reported in space group P65. 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° 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.

Item Type: Paper
Uncontrolled Keywords: bacterial protein caffeic acid caffeic acid derivative photoactive yellow protein, Bacteria visual proteins and pigments article chemical structure chemistry X ray crystallography Bacterial Proteins Caffeic Acids Crystallography X-Ray Models, Molecular Photoreceptors, Microbial
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Joshua-Tor lab
Depositing User: CSHL Librarian
Date: 2002
Date Deposited: 21 Mar 2012 19:47
Last Modified: 05 Sep 2017 19:15
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