Comparison between single-molecule and X-ray crystallography data on yeast F1-ATPase

• DOI: 10.1038/srep08773
• Publication Date: 2015-03-10T10:39:18Z
• Authors: Bradley C. Steel; Ashley L. Nord; Yamin Wang; Vijayakanth Pagadala; David M. Mueller; Richard M. Berry
• Keywords: Wild type

Abstract Single molecule studies in recent decades have elucidated the full chemo-mechanical cycle of F 1 -ATPase, mostly based on from thermophilic bacteria. In contrast, high-resolution crystal structures are only available for mitochondrial . Here we present high resolution single rotational data Saccharomyces cerevisiae , obtained using new throughput detection and analysis tools. Rotational presented wild type enzyme, a “liver” isoform six mutant forms yeast that previously been demonstrated to be less efficient or partially uncoupled. The wild-type isoforms show same qualitative features as Escherichia coli revealed delay at catalytic dwell associated decrease V max with magnitudes consistent level disruption seen structures. At least one shows un-observed ATP binding angle, potentially attributable slowed release ADP. We discuss correlation between results.