Abstract：
:Signal sequences target proteins for secretion from cells or for integration into cell membranes. As nascent proteins emerge from the ribosome, signal sequences are recognized by the signal recognition particle (SRP), which subsequently associates with its receptor (SR). In this complex, the SRP and SR stimulate each other's GTPase activity, and GTP hydrolysis ensures unidirectional targeting of cargo through a translocation pore in the membrane. To define the mechanism of reciprocal activation, we determined the 1.9 A structure of the complex formed between these two GTPases. The two partners form a quasi-two-fold symmetrical heterodimer. Biochemical analysis supports the importance of the extensive interaction surface. Complex formation aligns the two GTP molecules in a symmetrical, composite active site, and the 3'OH groups are essential for association, reciprocal activation and catalysis. This unique circle of twinned interactions is severed twice on hydrolysis, leading to complex dissociation after cargo delivery.
journal_name
Naturejournal_title
Natureauthors
Egea PF,Shan SO,Napetschnig J,Savage DF,Walter P,Stroud RMdoi
10.1038/nature02250keywords:
subject
Has Abstractpub_date
2004-01-15 00:00:00pages
215-21issue
6971eissn
0028-0836issn
1476-4687pii
nature02250journal_volume
427pub_type
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