2003
DOI: 10.1073/pnas.2436132100
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Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication

Abstract: Targeting of secretory and membrane proteins by the signal recognition particle (SRP) is evolutionarily conserved, and the multidomain protein SRP54 acts as the key player in SRP-mediated protein transport. Binding of a signal peptide to SRP54 at the ribosome is coordinated with GTP binding and subsequent complex formation with the SRP receptor. Because these functions are localized to distinct domains of SRP54, communication between them is essential. We report the crystal structures of SRP54 from the Archaeo… Show more

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Cited by 96 publications
(127 citation statements)
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“…In one crystal structure of the M domain (Thermus aquaticus; Keenan et al, 1998; Figure 6A, top), the residues line the top of one side of the signal sequence-binding groove. By contrast, in another crystal structure (Sulfolobus solfataricus; Rosendal et al, 2003), Figure 6B, top) the residues point away from the signal sequence-binding pocket. It is interesting to note that in the Keenan structure, two adjacent M Figure 5.…”
Section: Discussionmentioning
confidence: 88%
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“…In one crystal structure of the M domain (Thermus aquaticus; Keenan et al, 1998; Figure 6A, top), the residues line the top of one side of the signal sequence-binding groove. By contrast, in another crystal structure (Sulfolobus solfataricus; Rosendal et al, 2003), Figure 6B, top) the residues point away from the signal sequence-binding pocket. It is interesting to note that in the Keenan structure, two adjacent M Figure 5.…”
Section: Discussionmentioning
confidence: 88%
“…Moreover, the hydrophobic groove can (Rosendal et al, 2003). Because this conformational variability occurs in close juxtaposition to the 4.5S RNA, it is plausible that the RNA might monitor the occupancy of the signal sequence-binding pocket and transmit that information to the NG domain, thereby modulating its interaction with FtsY.…”
Section: Introductionmentioning
confidence: 99%
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“…The C-terminal domain of Ffh, called the ''M domain'' because of its high methionine content, comprises the RNAbinding site, 47,48 although some structural studies raise the possibility that the N domain may make contact with the RNA as well. [49][50][51][52] The M domain is mostly helical and contains a highly conserved hydrophobic loop (so-called finger loop), which is disordered in some crystal structures. 47,53 We found that the M domain is inherently flexible and binding of 4.5S RNA to Ffh stabilizes the M domain.…”
Section: Srp Structurementioning
confidence: 99%
“…2b). We docked available highresolution X-ray data 13,14 into the density and flexibly adjusted minor parts to build a molecular model of ribosome-bound E. coli SRP. Although the RNA of the X-ray data is truncated at loop C, we can follow it until loop E. Notably, the visible part of the 4.5S RNA has a kink of about 30u formed by the helix around nucleotide 72 next to loop C (Fig.…”
mentioning
confidence: 99%