Abstract:
:In all living cells, regulated passage across membranes of specific proteins occurs through a universally conserved secretory channel. In bacteria and chloroplasts, the energy for the mechanical work of moving polypeptides through that channel is provided by SecA, a regulated ATPase. Here, we use site-directed spin labeling and electron paramagnetic resonance spectroscopy to identify the interactive surface used by SecA for each of the diverse binding partners encountered during the dynamic cycle of export. Although the binding sites overlap, resolution at the level of aminoacyl side chains allows us to identify contacts that are unique to each partner. Patterns of constraint and mobilization of residues on that interactive surface suggest a conformational change that may underlie the coupling of ATP hydrolysis to precursor translocation.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Cooper DB,Smith VF,Crane JM,Roth HC,Lilly AA,Randall LLdoi
10.1016/j.jmb.2008.06.049subject
Has Abstractpub_date
2008-09-26 00:00:00pages
74-87issue
1eissn
0022-2836issn
1089-8638pii
S0022-2836(08)00765-1journal_volume
382pub_type
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