Khalili-Yazdi, Aliakbar Namjoshi, Sarita Hackett, Jesse Ghonaim, Nour Shilton, Brian H. Dataset for: Characterization of a Polypeptide Binding Site in the DEAD Motor of the SecA ATPase Peptides from a CNBr digest of signal-sequenceless maltose binding protein (MBP) were coupled to a surface plasmon resonance (SPR) chip. SecA-N95, SecA-N68, and SecA-DM (which consists of only the DEAD Motor domains, NBD1 and NBD2) bound to the immobilized peptides; ADP weakened the binding. SecA-DM, which lacks the “preprotein cross-linking domain” (PPXD), displayed the most extensive binding, while an MBP-PPXD chimera showed no binding, demonstrating that the PPXD does not contribute to the binding. The sequence specificity was characterized using oriented peptide libraries; these results enabled synthesis of a 20-residue peptide that was used to recapitulate the results obtained with MBP-derived peptides. The study shows there is a promiscuous and nucleotide-modulated peptide-binding site in the DEAD Motor domains of SecA. SecA;pre-protein binding;DEAD Motor;Biophysics;Synthetic Biology;Biochemistry;Plant Biology;Virology;Receptors and Membrane Biology;Computational Biology;Immunology;Neuroscience;Cell Development, Proliferation and Death;Molecular Biology;Evolutionary Biology;Signal Transduction;Cancer Cell Biology;Systems Biology;Structural Biology 2017-09-12
    https://wiley.figshare.com/articles/dataset/Dataset_for_Characterization_of_a_Polypeptide_Binding_Site_in_the_DEAD_Motor_of_the_SecA_ATPase/5350726
10.6084/m9.figshare.5350726.v1