4kf4
Crystal Structure of sfCherry
Structural highlights
FunctionRFP_DISSP Thought to play a role in photoprotection of the coral's resident symbiont microalgae's photosystems from photoinhibition caused by high light levels found near the surface of coral reefs. In deeper water, the fluorescence may be to convert blue light into longer wavelengths more suitable for use in photosynthesis by the microalgal symbionts.[1] Publication Abstract from PubMedA modular strategy for protein crystallization using split green fluorescent protein (GFP) as a crystallization partner is demonstrated. Insertion of a hairpin containing GFP beta-strands 10 and 11 into a surface loop of a target protein provides two chain crossings between the target and the reconstituted GFP compared with the single connection afforded by terminal GFP fusions. This strategy was tested by inserting this hairpin into a loop of another fluorescent protein, sfCherry. The crystal structure of the sfCherry-GFP(10-11) hairpin in complex with GFP(1-9) was determined at a resolution of 2.6 A. Analysis of the complex shows that the reconstituted GFP is attached to the target protein (sfCherry) in a structurally ordered way. This work opens the way to rapidly creating crystallization variants by reconstituting a target protein bearing the GFP(10-11) hairpin with a variety of GFP(1-9) mutants engineered for favorable crystallization. Split green fluorescent protein as a modular binding partner for protein crystallization.,Nguyen HB, Hung LW, Yeates TO, Terwilliger TC, Waldo GS Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2513-23. doi:, 10.1107/S0907444913024608. Epub 2013 Nov 19. PMID:24311592[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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