Conformational distribution and ultrafast base dynamics of leadzyme.
The dynamic nature of ribozymes represents a significant challenge in elucidating their structure-dynamics-function relationship. Here, using femtosecond time-resolved spectroscopy and other biophysical tools, we demonstrate that the active site of leadzyme does not have a unique structure, but rather samples an ensemble of conformations that undergo picosecond structural changes. Various base modifications have a profound context-dependent impact on the catalysis.
Kadakkuzha
Beena M
BM
Department of Molecular and Cell Biology, The University of Texas at Dallas, Richardson, Texas 75083-0688, USA.
Zhao
Liang
L
Xia
Tianbing
T
D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D018360:Crystallography, X-Ray; D006868:Hydrolysis; D007700:Kinetics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D016337:RNA, Catalytic / Q000737:chemistry* / Q000378:metabolism; D013057:Spectrum Analysis / Q000379:methods
D016337:RNA, Catalytic; C113411:leadzyme