What is it about?
We have shown for the first time, the conformational changes happening in SecA ATPase undergoing catalysis. Our results show that precursor binding domain and C-terminal segment are highly dynamic during ATP hydrolysis and work in a nucleotide dependent manner
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Why is it important?
ATP is energy currency of cell. Understanding how an ATPase hydrolyses this molecule is of fundamental importance for many biological processes like protein secretion. Proteins to be exported are synthesized as precursors with an N-terminal leader sequence and are translocated through the Sec pathway in E. coli. SecA, the adenosine triphosphatase (ATPase) of the Sec system, binds to the translocon SecYEG to form a translocase. In a process that is currently not well understood, this complex mediates chemomechanical conversion that results in translocation of precursor proteins across the cytoplasmic membrane
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This page is a summary of: Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis, Science Advances, October 2018, American Association for the Advancement of Science,
DOI: 10.1126/sciadv.aat8797.
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Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis
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Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis
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Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis
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Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis
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