Helix packing and subunit conformation in horse spleen apoferritin.
Abstract: An electron density map of horse spleen apoferritin at 0.28-nm (2.8 A) resolution and its preliminary interpretation have been described previously. Rigorous examination of this and newer maps at the same nominal resolution but calculated from more extensive data sets, including model building in a Richards' comparator, now allows us to report on structural features in more detail. We list inter-helical angles within and between neighbouring subunits, and describe a new short region of inter-subunit anti-parallel pleated sheet. A short section of electron density not properly accounted for in the first model has also been found. We also report on two alternative ways of connecting helical regions which account almost equally well for the observed electron density, and we assess these two alternative conformations and compare them with the conformations of other known proteins.
Publication Date: 1980-11-20 PubMed ID: 7432529DOI: 10.1038/288298a0Google Scholar: Lookup
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- Journal Article
Summary
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The research investigates the structural properties of apoferritin protein found in horse spleen through a rigorous examination of electron density maps. The study delves into the features like inter-helical angles and proposes potential structural changes, further comparing these presumed structures with conformations of other known proteins.
Background
- The researchers have studied the structure of a protein called apoferritin, which is found in the spleen of horses. To examine this protein, they constructed electron density maps at a resolution of 0.28-nm (2.8 A), which were based on extensive data sets.
Findings
- The study paid particular attention to the angles formed between protein helices (spiral sections of a protein) within a single unit of apoferritin and between different neighboring units. Different helices within a protein and between proteins interact to create the protein’s overall structure.
- Through this careful examination, researchers discovered a new short section of anti-parallel pleated sheet structure between different units. This type of structure, formed by protein strands, is common in many proteins but was not previously recognized in this one.
- Another new finding was a short section of electron density not accounted for in the first model, suggesting an area where the structure of the protein might be different than originally thought.
Alternative Model Assessments
- The researchers proposed two varied ways of connecting helical sections of the protein after having observed the electron density.
- Both these ways of connection give almost equally significant results in replicating the observed electron density, suggesting that each is a potential representation of the actual structure of the protein.
- These proposed alternative conformations are compared with known protein structures to refine understanding and support accuracy and validity of the models.
Conclusion
- The need for this study arises from the importance of understanding protein structure for understanding its function. Detailed knowledge about various structural features and comparisons with known protein structures helps in predicting protein functionality and can be vital in biomedical research.
Cite This Article
APA
Clegg GA, Stansfield RF, Bourne PE, Harrison PM.
(1980).
Helix packing and subunit conformation in horse spleen apoferritin.
Nature, 288(5788), 298-300.
https://doi.org/10.1038/288298a0 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Apoproteins
- Ferritins
- Horses
- Hydrogen Bonding
- Macromolecular Substances
- Protein Conformation
- Spleen
- X-Ray Diffraction
Citations
This article has been cited 4 times.- Mura C, Candelier E, Xie L. A Tribute to Phil Bourne-Scientist and Human. Biomolecules 2023 Jan 16;13(1).
- Yamanaka M, Mashima T, Ogihara M, Okamoto M, Uchihashi T, Hirota S. Construction of ferritin hydrogels utilizing subunit-subunit interactions. PLoS One 2021;16(11):e0259052.
- Thompson TB, Chou KC, Zheng C. Analysis of the loop-helix interaction in bundle motif protein structures. J Protein Chem 1995 Oct;14(7):559-66.
- Chou KC, Maggiora GM, Némethy G, Scheraga HA. Energetics of the structure of the four-alpha-helix bundle in proteins. Proc Natl Acad Sci U S A 1988 Jun;85(12):4295-9.
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