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

Journal of Molecular Biology

Volumn 364, Issue 3, 2006, Pages 259-265

  Zimmer, Jochen ^a   Li, Weikai ^a   Rapoport, Tom A ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

protein translocation; SecA; signal peptide binding; X ray structure

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; DIMER; MONOMER; NUCLEOTIDE BINDING PROTEIN; POLYPEPTIDE; PROTEIN SECA; PROTEIN SUBUNIT;

ALPHA HELIX; ARTICLE; BACILLUS SUBTILIS; BETA CHAIN; CRYSTAL STRUCTURE; DIMERIZATION; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; SURFACE PROPERTY;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS);

EID: 33750821188     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.08.044     Document Type: Article

References (26)

1. Brundage L., Hendrick J.P., Schiebel E., Driessen A.J., and Wickner W. The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell 62 (1990) 649-657
2. Cannon K.S., Or E., Clemons Jr. W.M., Shibata Y., and Rapoport T.A. Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. J. Cell. Biol. 169 (2005) 219-225
3. Economou A., and Wickner W. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78 (1994) 835-843
4. Osborne A.R., Rapoport T.A., and van den Berg B. Protein translocation by the Sec61/SecY channel. Annu. Rev. Cell Dev. Bio. 21 (2005) 529-550
5. Vrontou E., and Economou A. Structure and function of SecA, the preprotein translocase nanomotor. Biochim. Biophys. Acta 1694 (2004) 67-80
6. de Keyzer J., van der Does C., and Driessen A.J. The bacterial translocase: a dynamic protein channel complex. Cell. Mol. Life Sci. 60 (2003) 2034-2052
7. Tanner N.K., and Linder P. DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol. Cell 8 (2001) 251-262
8. Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B., and Deisenhofer J. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science 297 (2002) 2018-2026
9. Ye J., Osborne A.R., Groll M., and Rapoport T.A. RecA-like motor ATPases-lessons from structures. Biochim. Biophys. Acta 1659 (2004) 1-18
10. Sharma V., Arockiasamy A., Ronning D.R., Savva C.G., Holzenburg A., Braunstein M., et al. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase. Proc. Natl Acad. Sci. USA 100 (2003) 2243-2248
11. Osborne A.R., Clemons Jr. W.M., and Rapoport T.A. A large conformational change of the translocation ATPase SecA. Proc. Natl Acad. Sci. USA 101 (2004) 10932-10937
12. Kimura E., Akita M., Matsuyama S., and Mizushima S. Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli. J. Biol. Chem. 266 (1991) 6600-6606
13. Or E., Navon A., and Rapoport T. Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane. EMBO J. 21 (2002) 4470-4479
14. Or E., Boyd D., Gon S., Beckwith J., and Rapoport T. The bacterial ATPase SecA functions as a monomer in protein translocation. J Biol Chem 280 (2005) 9097-9105
15. Ding H., Hunt J.F., Mukerji I., and Oliver D. Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution. Biochemistry 42 (2003) 8729-8738
16. Jilaveanu L.B., and Oliver D. SecA dimer cross-linked at its subunit interface is functional for protein translocation. J. Bacteriol. 188 (2006) 335-338
17. Jilaveanu L.B., Zito C.R., and Oliver D. Dimeric SecA is essential for protein translocation. Proc. Natl Acad. Sci. U S A 102 (2005) 7511-7516
18. Weinkauf S., Hunt J.F., Scheuring J., Henry L., Fak J., Oliver D.B., and Deisenhofer J. Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis. Acta Crystallog. sect. D 57 (2001) 559-565
19. Schlichting I., and Reinstein J. pH influences fluoride coordination number of the AlFx phosphoryl transfer transition state analog. Nature Struct. Biol. 6 (1999) 721-723
20. Papanikou E., Karamanou S., Baud C., Frank M., Sianidis G., Keramisanou D., et al. Identification of the preprotein binding domain of SecA. J. Biol. Chem. 280 (2005) 43209-43217
21. Velankar S.S., Soultanas P., Dillingham M.S., Subramanya H.S., and Wigley D.B. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97 (1999) 75-84
22. Keramisanou D., Biris N., Gelis I., Sianidis G., Karamanou S., Economou A., and Kalodimos C.G. Disorder-order folding transitions underlie catalysis in the helicase motor of SecA. Nature Struct. Mol. Biol. 13 (2006) 594-602
23. Otwinowsky Z., and Minor W. Processing X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
24. Cowtan K.D., and Main P. Phase combination and cross-validation in iterated density-modification calculations. Acta Crystallog. sect. D 52 (1996) 43-48
25. Jones T.A., Zou J.Y., and Cowan S.W. Kjeldgaard., Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
26. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallog. sect. D 54 (1998) 905-921