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zeige Details Freymann, Douglas M., Keenan, Robert J., ... Structure of the conserved GTPase domain of the signal recognition particle
in: Nature . - London [u.a.] : Nature Publising Group, ISSN 1476-4687, Vol. 385, No. 6614 (1997), p. 361-364
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1997
The signal-recognition particle (SRP) and its receptor (SR) function in the co-translational targeting of nascent protein–ribosome complexes to the membrane translocation apparatus1. The SRP protein subunit (termed Ffh in bacteria) that recognizes the signal sequence of nascent polypeptides is a GTPase, as is the SR-α subunit (termed FtsY)2,3. Ffh and FtsY interact directly, each stimulating the GTP hydrolysis activity of the other4. The sequence of Ffh suggests three domains: an amino-terminal N domain of unknown function, a central GTPase G domain, and a methionine-rich M domain that binds both SRP RNA and signal peptides5,6. Sequence conservation suggests that structurally similar N and G domains are present in FtsY7,8. Here we report the structure of the nucleotide-free form of the NG fragment of Ffh. Consistent with a role for apo Ffh in protein targeting, the side chains of the empty active-site pocket form a tight network of interactions which may stabilize the nucleotide-free protein. The structural relationship between the two domains suggests that the N domain senses or controls the nucleotide occupancy of the GTPase domain. A structural subdomain unique to these evolutionarily conserved GTPases constitutes them as a distinct subfamily in the GTPase superfamily9.
beteiligte Personen: Freymann, Douglas M. , Keenan, Robert J. , Stroud, Robert M. , Walter, Peter
Format: Elektronisch
Erschienen: 1997.
Serie: Nature Archives 1869 - 2007 [Dig. Serial]
Schlagwörter:
URL: http://dx.doi.org/10.1038/385361a0

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Verfasser Titel Jahr
zeige Details Freymann, Douglas M., Keenan, Robert J., ... Functional changes in the structure of the SRP GTPase on binding GDP and Mg<sup>2+</sup>GDP
in: Nature structural biology . - New York, NY : Nature America, ISSN 1072-8368, Vol. 6, No. 8 (1999), p. 793-801
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in: Nature . - London [u.a.] : Nature Publising Group, ISSN 1476-4687, Vol. 385, No. 6614 (1997), p. 365-368
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