Fluorescence energy transfer between Tyr 69 and Cys 374 in actin.
Modification of Tyr 69 with the chromophore dansyl chloride was found to completely block exchange of the bound ATP on actin. No significant conformational change was detected in the actin after labelling thus indicating that the dansyl chloride is close to and probably sterically blocks the ATP site. The distance separating dansyl chloride attached to Tyr 69 and IAEDANS attached to Cys 374 on actin was found using fluorescence energy transfer to be 3.9 nm. This result is consistent with the known distance between the ATP site and Cys 374.
D000199:Actins / Q000032:analysis*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D003553:Cystine / Q000032:analysis*; D003619:Dansyl Compounds / Q000032:analysis; D003850:Deoxyribonuclease I / Q000378:metabolism; D004735:Energy Transfer; D005453:Fluorescence; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D014443:Tyrosine / Q000032:analysis*
D000199:Actins; D003619:Dansyl Compounds; D014443:Tyrosine; D003553:Cystine; D000255:Adenosine Triphosphate; D003850:Deoxyribonuclease I; C029038:dansyl chloride