1kou
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(New page: 200px<br /><applet load="1kou" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kou, resolution 1.16Å" /> '''Crystal Structure of...)
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Revision as of 17:24, 20 November 2007
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Crystal Structure of the Photoactive Yellow Protein Reconstituted with Caffeic Acid at 1.16 A Resolution
Overview
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.
About this Structure
1KOU is a Single protein structure of sequence from Halorhodospira halophila with DHC and NBU as ligands. Full crystallographic information is available from OCA.
Reference
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
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