Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation.
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ABSTRACT:
SUBMITTER: Heidi Linda Schubert
PROVIDER: EMPIAR-10382 | biostudies-other |
REPOSITORIES: biostudies-other
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Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation.
Han Han H Schubert Heidi L HL McCullough John J Monroe Nicole N Purdy Michael D MD Yeager Mark M Sundquist Wesley I WI Hill Christopher P CP
The Journal of biological chemistry 20191125 2
Many members of the AAA+ ATPase family function as hexamers that unfold their protein substrates. These AAA unfoldases include spastin, which plays a critical role in the architecture of eukaryotic cells by driving the remodeling and severing of microtubules, which are cytoskeletal polymers of tubulin subunits. Here, we demonstrate that a human spastin binds weakly to unmodified peptides from the C-terminal segment of human tubulin α1A/B. A peptide comprising alternating glutamate and tyrosine r ...[more]
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