Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers
- PMID:16581049
- DOI: 10.1016/j.chemphyslip.2006.02.004
Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers
Abstract
The folding mechanism of outer membrane proteins (OMPs) of Gram-negative bacteria into lipid bilayers has been studied using OmpA of E. coli and FomA of F. nucleatum as examples. Both, OmpA and FomA are soluble in unfolded form in urea and insert and fold into phospholipid bilayers upon strong dilution of the denaturant urea. OmpA is a structural protein and forms a small ion channel, composed of an 8-stranded transmembrane beta-barrel domain. FomA is a voltage-dependent porin, predicted to form a 14 stranded beta-barrel. Both OMPs fold into a range of model membranes of very different phospholipid compositions. Three membrane-bound folding intermediates of OmpA were discovered in folding studies with dioleoylphosphatidylcholine bilayers that demonstrated a highly synchronized mechanism of secondary and tertiary structure formation of beta-barrel membrane proteins. A study on FomA folding into lipid bilayers indicated the presence of parallel folding pathways for OMPs with larger transmembrane beta-barrels.
Similar articles
- The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways.Pocanschi CL, Apell HJ, Puntervoll P, Høgh B, Jensen HB, Welte W, Kleinschmidt JH.Pocanschi CL, et al.J Mol Biol. 2006 Jan 20;355(3):548-61. doi: 10.1016/j.jmb.2005.10.060. Epub 2005 Nov 9.J Mol Biol. 2006.PMID:16310217
- The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential.Patel GJ, Behrens-Kneip S, Holst O, Kleinschmidt JH.Patel GJ, et al.Biochemistry. 2009 Nov 3;48(43):10235-45. doi: 10.1021/bi901403c.Biochemistry. 2009.PMID:19780589
- The lipid bilayer-inserted membrane protein BamA of Escherichia coli facilitates insertion and folding of outer membrane protein A from its complex with Skp.Patel GJ, Kleinschmidt JH.Patel GJ, et al.Biochemistry. 2013 Jun 11;52(23):3974-86. doi: 10.1021/bi400103t. Epub 2013 May 24.Biochemistry. 2013.PMID:23641708
- Membrane protein folding on the example of outer membrane protein A of Escherichia coli.Kleinschmidt JH.Kleinschmidt JH.Cell Mol Life Sci. 2003 Aug;60(8):1547-58. doi: 10.1007/s00018-003-3170-0.Cell Mol Life Sci. 2003.PMID:14513830Free PMC article.Review.
- Folding of β-barrel membrane proteins in lipid bilayers - Unassisted and assisted folding and insertion.Kleinschmidt JH.Kleinschmidt JH.Biochim Biophys Acta. 2015 Sep;1848(9):1927-43. doi: 10.1016/j.bbamem.2015.05.004. Epub 2015 May 14.Biochim Biophys Acta. 2015.PMID:25983306Review.
Cited by
- An unfolding story of helical transmembrane proteins.Renthal R.Renthal R.Biochemistry. 2006 Dec 12;45(49):14559-66. doi: 10.1021/bi0620454.Biochemistry. 2006.PMID:17144649Free PMC article.Review.
- Complete proteome of a quinolone-resistant Salmonella Typhimurium phage type DT104B clinical strain.Correia S, Nunes-Miranda JD, Pinto L, Santos HM, de Toro M, Sáenz Y, Torres C, Capelo JL, Poeta P, Igrejas G.Correia S, et al.Int J Mol Sci. 2014 Aug 15;15(8):14191-219. doi: 10.3390/ijms150814191.Int J Mol Sci. 2014.PMID:25196519Free PMC article.
- Classifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members.Mahoney TF, Ricci DP, Silhavy TJ.Mahoney TF, et al.J Bacteriol. 2016 Jun 27;198(14):1984-92. doi: 10.1128/JB.00263-16. Print 2016 Jul 15.J Bacteriol. 2016.PMID:27161117Free PMC article.
- bam Lipoproteins Assemble BamA in vitro.Hagan CL, Westwood DB, Kahne D.Hagan CL, et al.Biochemistry. 2013 Sep 3;52(35):6108-13. doi: 10.1021/bi400865z. Epub 2013 Aug 21.Biochemistry. 2013.PMID:23919461Free PMC article.
- Renaturing membrane proteins in the lipid cubic phase, a nanoporous membrane mimetic.Li D, Caffrey M.Li D, et al.Sci Rep. 2014 Jul 24;4:5806. doi: 10.1038/srep05806.Sci Rep. 2014.PMID:25055873Free PMC article.
Publication types
MeSH terms
Substances
Related information
LinkOut - more resources
Full Text Sources
Molecular Biology Databases