F1F0-ATP synthase-stalking mind and imagination
- PMID: 11768294
- DOI: 10.1023/a:1005567717821
F1F0-ATP synthase-stalking mind and imagination
Abstract
Electron microscopy together with image analysis has been used to study the structure of the intact F1F0-ATPsynthase from Escherichia coli. A procedure has been developed which allows preparation of detergent-free enzyme. Aside from the well known two-domain structure, images of F1F0 prepared by this procedure show a number of additional features, including a second stalk, which can be seen extending all the way from the F0 to the top of the F1 in some images, and a small protein on the very top of the F1, which has been identified as the delta subunit by decoration with a monoclonal antibody. In light of these results, a refined model of the subunit arrangement of the complex is presented.
Similar articles
-
Electron microscopic evidence of two stalks linking the F1 and F0 parts of the Escherichia coli ATP synthase.Biochim Biophys Acta. 1998 Jun 10;1365(1-2):93-7. doi: 10.1016/s0005-2728(98)00048-6. Biochim Biophys Acta. 1998. PMID: 9693727 Review.
-
Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy.Biochemistry. 1990 Jun 5;29(22):5339-43. doi: 10.1021/bi00474a019. Biochemistry. 1990. PMID: 2200506
-
The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens.FEBS Lett. 1987 Jul 27;219(2):274-8. doi: 10.1016/0014-5793(87)80234-x. FEBS Lett. 1987. PMID: 2886365
-
Electron microscopy of the F1F0 ATP synthase: from structure to function.Microsc Res Tech. 1994 Mar 1;27(4):294-306. doi: 10.1002/jemt.1070270405. Microsc Res Tech. 1994. PMID: 8186448 Review.
-
Localization of the delta subunit in the Escherichia coli F(1)F(0)-ATPsynthase by immuno electron microscopy: the delta subunit binds on top of the F(1).J Mol Biol. 2000 Jan 21;295(3):387-91. doi: 10.1006/jmbi.1999.3381. J Mol Biol. 2000. PMID: 10623533
Cited by
-
Invadolysin, a conserved lipid-droplet-associated metalloproteinase, is required for mitochondrial function in Drosophila.J Cell Sci. 2013 Oct 15;126(Pt 20):4769-81. doi: 10.1242/jcs.133306. Epub 2013 Aug 13. J Cell Sci. 2013. PMID: 23943867 Free PMC article.
-
Low resolution structure of subunit b (b (22-156)) of Escherichia coli F(1)F(O) ATP synthase in solution and the b-delta assembly.J Bioenerg Biomembr. 2008 Aug;40(4):245-55. doi: 10.1007/s10863-008-9154-x. Epub 2008 Jul 31. J Bioenerg Biomembr. 2008. PMID: 18668355
-
Electron cryomicroscopy of membrane proteins: specimen preparation for two-dimensional crystals and single particles.Micron. 2011 Feb;42(2):107-16. doi: 10.1016/j.micron.2010.07.004. Epub 2010 Jul 16. Micron. 2011. PMID: 20678942 Free PMC article. Review.
-
Individual interactions of the b subunits within the stator of the Escherichia coli ATP synthase.J Biol Chem. 2013 Aug 23;288(34):24465-79. doi: 10.1074/jbc.M113.465633. Epub 2013 Jul 11. J Biol Chem. 2013. PMID: 23846684 Free PMC article.
-
Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase.J Bacteriol. 2009 Dec;191(24):7538-44. doi: 10.1128/JB.00540-09. Epub 2009 Oct 9. J Bacteriol. 2009. PMID: 19820091 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources