DOI: 10.1016/j.jmb.2006.08.044. A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA

A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA

10.1016/j.jmb.2006.08.044

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Zimmer, J., Li, W., & Rapoport, T. A. (2006). A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA. Journal of Molecular Biology, 364(3), 259â265.

Authors 3

Jochen Zimmer (first)
Weikai Li (additional)
Tom A. Rapoport (additional)

References 26 Referenced 71

10.1016/0092-8674(90)90111-Q / Cell / The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation by Brundage (1990)
10.1083/jcb.200412019 / J. Cell. Biol. / Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY by Cannon (2005)
10.1016/S0092-8674(94)90582-7 / Cell / SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion by Economou (1994)
10.1146/annurev.cellbio.21.012704.133214 / Annu. Rev. Cell Dev. Bio. / Protein translocation by the Sec61/SecY channel by Osborne (2005)
10.1016/j.bbamcr.2004.06.003 / Biochim. Biophys. Acta / Structure and function of SecA, the preprotein translocase nanomotor by Vrontou (2004)
10.1007/s00018-003-3006-y / Cell. Mol. Life Sci. / The bacterial translocase: a dynamic protein channel complex by de Keyzer (2003)
10.1016/S1097-2765(01)00329-X / Mol. Cell / DExD/H box RNA helicases: from generic motors to specific dissociation functions by Tanner (2001)
10.1126/science.1074424 / Science / Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA by Hunt (2002)
10.1016/j.bbabio.2004.06.003 / Biochim. Biophys. Acta / RecA-like motor ATPases–lessons from structures by Ye (2004)
10.1073/pnas.0538077100 / Proc. Natl Acad. Sci. USA / Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase by Sharma (2003)
10.1073/pnas.0401742101 / Proc. Natl Acad. Sci. USA / A large conformational change of the translocation ATPase SecA by Osborne (2004)
10.1016/S0021-9258(18)38159-6 / J. Biol. Chem. / Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli by Kimura (1991)
10.1093/emboj/cdf471 / EMBO J. / Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane by Or (2002)
10.1074/jbc.M413947200 / J Biol Chem / The bacterial ATPase SecA functions as a monomer in protein translocation by Or (2005)
10.1021/bi0342057 / Biochemistry / Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution by Ding (2003)
10.1128/JB.188.1.335-338.2006 / J. Bacteriol. / SecA dimer cross-linked at its subunit interface is functional for protein translocation by Jilaveanu (2006)
10.1073/pnas.0502774102 / Proc. Natl Acad. Sci. U S A / Dimeric SecA is essential for protein translocation by Jilaveanu (2005)
10.1107/S0907444901001202 / Acta Crystallog. sect. D / Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis by Weinkauf (2001)
10.1038/11485 / Nature Struct. Biol. / pH influences fluoride coordination number of the AlFx phosphoryl transfer transition state analog by Schlichting (1999)
10.1074/jbc.M509990200 / J. Biol. Chem. / Identification of the preprotein binding domain of SecA by Papanikou (2005)
10.1016/S0092-8674(00)80716-3 / Cell / Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism by Velankar (1999)
10.1038/nsmb1108 / Nature Struct. Mol. Biol. / Disorder-order folding transitions underlie catalysis in the helicase motor of SecA by Keramisanou (2006)
10.1016/S0076-6879(97)76066-X / Methods Enzymol. / Processing X-ray diffraction data collected in oscillation mode by Otwinowsky (1997)
10.1107/S090744499500761X / Acta Crystallog. sect. D / Phase combination and cross-validation in iterated density-modification calculations by Cowtan (1996)
10.1107/S0108767390010224 / Acta Crystallog. sect. A / Kjeldgaard., Improved methods for building protein models in electron density maps and the location of errors in these models by Jones (1991)
10.1107/S0907444998003254 / Acta Crystallog. sect. D / Crystallography & NMR system: A new software suite for macromolecular structure determination by Brunger (1998)

Dates

Type	When
Created	19 years ago (Aug. 25, 2006, 5:40 p.m.)
Deposited	1 year, 6 months ago (Feb. 23, 2024, noon)
Indexed	6 months, 2 weeks ago (Feb. 20, 2025, 9:37 p.m.)
Issued	18 years, 9 months ago (Dec. 1, 2006)
Published	18 years, 9 months ago (Dec. 1, 2006)
Published Print	18 years, 9 months ago (Dec. 1, 2006)

Funders 1

National Institutes of Health 10.13039/100000002
Region: Americas
gov (National government)
Labels3
1. Institutos Nacionales de la Salud
2. US National Institutes of Health
3. NIH

BibTeX

@article{Zimmer_2006, title={A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA}, volume={364}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2006.08.044}, DOI={10.1016/j.jmb.2006.08.044}, number={3}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Zimmer, Jochen and Li, Weikai and Rapoport, Tom A.}, year={2006}, month=dec, pages={259–265} }

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      "value": "Copyright \u00a9 2006 Elsevier Ltd. All rights reserved.",
      "name": "copyright",
      "label": "Copyright"
    }
  ]
}