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Structure of a complex of the ATPase SecA and the protein-translocation channel.
Open accessAbstract
Most proteins are secreted from bacteria by the interaction of the cytoplasmic SecA ATPase with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 ångström (A), obtained for components from Thermotoga maritima. One copy of SecA in an intermediate state of ATP hydrolysis is bound to one molecule of the SecY complex. Both partners undergo important conformational changes on interaction. The polypeptide-cross-linking domain of SecA makes a large conformational change that could capture the translocation substrate in a 'clamp'. Polypeptide movement through the SecY channel could be achieved by the motion of a 'two-helix finger' of SecA inside the cytoplasmic funnel of SecY, and by the coordinated tightening and widening of SecA's clamp above the SecY pore. SecA binding generates a 'window' at the lateral gate of the SecY channel and it displaces the plug domain, preparing the channel for signal sequence binding and channel opening.
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“The Sec translocon in bacteria and eukaryotes is organized as a highly modular protein complex and multiple different entities have been structurally and biochemically characterized (Zimmer et al., 2008; Boy and Koch, 2009; Frauenfeld et al., 2011; Denks et al., 2014; Komar et al., 2016; Kater et al., 2019).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Zimmer et al., 2008
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“SecYEG was furthermore found in heterotetrameric complexes with SecA (Zimmer et al., 2008) or YidC (Boy and Koch, 2009; Sachelaru et al., 2017), and as heterohexameric complexes with SecDFYajC (Duong and Wickner, 1997) or FtsY-SRP-RNCs (Jomaa et al., 2017).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Zimmer et al., 2008
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Metadata
- Authors
- Zimmer, J., Nam, Y., & Rapoport, T. A.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Rapoport, Tom A.
- Venue
- Nature
- Published
- 2008-10
- Volume
- 455
- Issue
- 7215
- Pages
- 936-943
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7164768
- OpenAlex
- W1968636401
- Cited by
- 459
- References
- 64
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 12 · 2023: 8 · 2022: 20 · 2021: 16 · 2020: 27 · 2019: 41 · 2018: 24 · 2017: 20 · 2016: 30 · 2015: 29 · 2014: 29 · 2013: 27 · 2012: 41
- FWCI
- 23.38
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (R01GM052586)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- SecA ATPase, protein translocation, crystal structure, Thermotoga maritima, conformational change, channel gating, bacterial protein secretion
- MeSH terms
- SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Adenosine Triphosphate, Bacillus subtilis, Bacterial Proteins, Hydrolysis, Models, Biological, Models, Molecular, Movement, Protein Binding, Protein Conformation, Structure-Activity Relationship, Crystallography, X-Ray, Thermotoga maritima, Protein Transport, Protein Sorting Signals, Membrane Transport Proteins, Multiprotein Complexes
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