Structural highlights
Function[PYP_HALHA] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA 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. Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 A resolution.,van Aalten DM, Crielaard W, Hellingwerf KJ, Joshua-Tor L Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):585-90. Epub 2002, Mar 22. PMID:11914481[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References | ||||||||||||||||||||||
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