Evidence map›Paper›PMID 1330536›Full record

ArticleThe EMBO journal1992

Isolation and cloning of Omp alpha, a coiled-coil protein spanning the periplasmic space of the ancestral eubacterium Thermotoga maritima.

A M Engel, Z Cejka, A Lupas, F Lottspeich, W Baumeister

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. The cell envelope ofProceedings of the National Academy of Sciences of the United States of America · 2023
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  3. A multidomain connector links the outer membrane and cell wall in phylogenetically deep-branching bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Binding ofAutophagy · 2020
    Article
  7. Progeny production in the periplasm of Thermosipho globiformans.Extremophiles : life under extreme conditions · 2017
    Article
  8. Coiled-coils: The long and short of it.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  9. Article
  10. Article
  11. Thermus thermophilus as biological model.Extremophiles : life under extreme conditions · 2009
    Review
  12. Article
  13. A voyage to the inner space of cells.Protein science : a publication of the Protein Society · 2005
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

A M EngelMax-Planck-Institut für Biochemie, Martinsried, Germany.
Z Cejka
A Lupas
F Lottspeich
W Baumeister
Max Planck Institute of Biochemistry · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have discovered a new oligomeric protein component associated with the outer membrane of the ancestral eubacterium Thermotoga maritima. In electron micrographs, the protein, Omp alpha, appears as a rod-shaped spacer that spans the periplasm, connecting the outer membrane to the inner cell body. Purification, biochemical characterization and sequencing of Omp alpha suggest that it is a homodimer composed of two subunits of 380 amino acids with a calculated M(r) of 43,000 and a pI of 4.54. The sequence of the omp alpha gene indicates a tripartite organization of the protein with a globular NH2-terminal domain of 64 residues followed by a putative coiled-coil segment of 300 residues and a COOH-terminal, membrane-spanning segment. The predicted length of the coiled-coil segment (45 nm) correlates closely with the spacing between the inner and outer membranes. Despite sequence similarity to a large number of coiled-coil proteins and high scores in a coiled-coil prediction algorithm, the sequence of the central rod-shaped domain of Omp alpha does not have the typical 3.5 periodicity of coiled-coil proteins but rather has a periodicity of 3.58 residues. Such a periodicity was also found in the central domain of staphylococcal M protein and beta-giardin and might be indicative of a subclass of fibrous proteins with packing interactions that are distinct from the ones seen in other two-stranded coiled-coils.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBase SequenceCloning, MolecularDNA, BacterialElectrophoresis, Polyacrylamide GelFreeze FracturingGram-Negative Anaerobic BacteriaImage Processing, Computer-AssistedMicroscopy, ElectronMolecular Sequence DataPolymerase Chain ReactionPorinsProtein Structure, SecondaryBacterial Outer Membrane ProteinsDNA, BacterialOMPA outer membrane proteinsPorins

Identifiers

PMID1330536
PMCPMC557011
OpenAlexW217084825

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.