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Cited by 255

The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.

Heterodimeric GTPase Core of the SRP Targeting Complex

Open access
Focia, Pamela J., Shepotinovskaya, Irina V., Seidler, James A., Freymann, Douglas M.·2004·Science

Abstract

Two structurally homologous guanosine triphosphatase (GTPase) domains interact directly during signal recognition particle (SRP)–mediated cotranslational targeting of proteins to the membrane. The 2.05 angstrom structure of a complex of the NG GTPase domains of Ffh and FtsY reveals a remarkably symmetric heterodimer sequestering a composite active site that contains two bound nucleotides. The structure explains the coordinate activation of the two GTPases. Conformational changes coupled to formation of their extensive interface may function allosterically to signal formation of the targeting complex to the signal-sequence binding site and the translocon. We propose that the complex represents a molecular “latch” and that its disengagement is regulated by completion of assembly of the GTPase active site.

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Crossref · 10.1126/science.1090827

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Metadata

Authors
Focia, P. J., Shepotinovskaya, I. V., Seidler, J. A., & Freymann, D. M.
Venue
Science
Published
2004-01-16
Volume
303
Issue
5656
Pages
373-377
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2041781518
Cited by
255
References
33
FWCI
9.07
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Heterodimeric GTPase Core of the SRP Targeting Complex. https://app.cochat.ai/papers/10.1126/science.1090827
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Focia, P. J., Shepotinovskaya, I. V., Seidler, J. A., & Freymann, D. M. (2004). Heterodimeric GTPase Core of the SRP Targeting Complex. Science. https://doi.org/10.1126/science.1090827

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.