Kindling fluorescent protein from Anemonia sulcata: dark-state structure at 1.38 A resolution.

作者: Michael L. Quillin , David M. Anstrom , Xiaokun Shu , Shannon O'Leary , Karen Kallio

DOI: 10.1021/BI047644U

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摘要: When the nonfluorescent chromoprotein asFP595 from Anemonia sulcata is subjected to sufficiently intense illumination near absorbance maximum (λabsmax = 568 nm), it undergoes a remarkable transition, termed “kindling”, long-lived fluorescent state (λemmax 595 nm). In dark recovery phase, kindled relaxes thermally on time scale of seconds or can instantly be reverted upon at 450 nm. The kindling phenomenon enhanced by Ala143 → Gly point mutation, which slows constant 100 s room temperature and increases fluorescence quantum yield. To investigate chemical nature chromophore possible role isomerization in phenomenon, we determined crystal structure “kindling protein” asFP595-A143G (KFP) dark-adapted 1.38 A resolution K. chromophore, derived Met63-Tyr64-Gly65 tripeptide, closely resembles that chromoprot...

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