Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA - PubMed (original) (raw)
. 1995 Jul 28;250(5):617-26.
doi: 10.1006/jmbi.1995.0403.
Affiliations
- PMID: 7623380
- DOI: 10.1006/jmbi.1995.0403
Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA
R Koebnik et al. J Mol Biol. 1995.
Abstract
The two-domain, 325 residue outer membrane protein OmpA is one of the most abundant proteins of Escherichia coli, playing a role in the maintenance of the integrity of the cell surface. The N-terminal domain, consisting of about 170 amino acid residues, is embedded in the membrane, presumably in the form of a beta-barrel consisting of eight amphipathic transmembrane strands. Pairs of these proposed transmembrane strands were permuted at the DNA level, in order to dissect the process of membrane assembly. All three possible circular permutations led to variants, which were, in comparison with the wild-type protein, less efficiently assembled. In contrast, no membrane assembly could be detected in any of 18 non-circularly permuted variants. We take this as an indication that the "right" (wild-type) order of beta-strands is a necessary and sufficient prerequisite for at least partially successful membrane assembly. This may be the consequence of packing constraints and/or a failure to adopt the wild-type arrangement of beta-strands, which require crossing of the periplasmic turns.
Similar articles
- In vivo membrane assembly of split variants of the E.coli outer membrane protein OmpA.
Koebnik R. Koebnik R. EMBO J. 1996 Jul 15;15(14):3529-37. EMBO J. 1996. PMID: 8670856 Free PMC article. - Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study.
Qu J, Behrens-Kneip S, Holst O, Kleinschmidt JH. Qu J, et al. Biochemistry. 2009 Jun 9;48(22):4926-36. doi: 10.1021/bi9004039. Biochemistry. 2009. PMID: 19382746 - Molecular mechanism of ferricsiderophore passage through the outer membrane receptor proteins of Escherichia coli.
Chakraborty R, Storey E, van der Helm D. Chakraborty R, et al. Biometals. 2007 Jun;20(3-4):263-74. doi: 10.1007/s10534-006-9060-9. Epub 2006 Dec 22. Biometals. 2007. PMID: 17186377 Review. - Insights into the structure and assembly of Escherichia coli outer membrane protein A.
Reusch RN. Reusch RN. FEBS J. 2012 Mar;279(6):894-909. doi: 10.1111/j.1742-4658.2012.08484.x. Epub 2012 Feb 10. FEBS J. 2012. PMID: 22251410 Free PMC article. Review.
Cited by
- Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms.
Wang X, Peterson JH, Bernstein HD. Wang X, et al. mBio. 2021 May 4;12(3):e00597-21. doi: 10.1128/mBio.00597-21. mBio. 2021. PMID: 33947759 Free PMC article. - Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA.
Danoff EJ, Fleming KG. Danoff EJ, et al. Biochemistry. 2017 Jan 10;56(1):47-60. doi: 10.1021/acs.biochem.6b00809. Epub 2016 Dec 21. Biochemistry. 2017. PMID: 28001375 Free PMC article. - Outer membrane protein design.
Slusky JS. Slusky JS. Curr Opin Struct Biol. 2017 Aug;45:45-52. doi: 10.1016/j.sbi.2016.11.003. Epub 2016 Nov 26. Curr Opin Struct Biol. 2017. PMID: 27894013 Free PMC article. Review. - Computational redesign of the lipid-facing surface of the outer membrane protein OmpA.
Stapleton JA, Whitehead TA, Nanda V. Stapleton JA, et al. Proc Natl Acad Sci U S A. 2015 Aug 4;112(31):9632-7. doi: 10.1073/pnas.1501836112. Epub 2015 Jul 21. Proc Natl Acad Sci U S A. 2015. PMID: 26199411 Free PMC article. - Polar localization of PhoN2, a periplasmic virulence-associated factor of Shigella flexneri, is required for proper IcsA exposition at the old bacterial pole.
Scribano D, Petrucca A, Pompili M, Ambrosi C, Bruni E, Zagaglia C, Prosseda G, Nencioni L, Casalino M, Polticelli F, Nicoletti M. Scribano D, et al. PLoS One. 2014 Feb 27;9(2):e90230. doi: 10.1371/journal.pone.0090230. eCollection 2014. PLoS One. 2014. PMID: 24587292 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases