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  A coiled-coil motif that sequesters ions to the hydrophobic core

Hartmann, M., Ridderbusch, O., Zeth, K., Albrecht, R., Testa, O., Woolfson, D., et al. (2009). A coiled-coil motif that sequesters ions to the hydrophobic core. Proceedings of the National Academy of Sciences of the United States of America, 106(40), 16950-16955. doi:10.1073/pnas.0907256106.

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 Creators:
Hartmann, MD1, Author           
Ridderbusch, O1, Author           
Zeth, K1, Author           
Albrecht, R1, Author           
Testa, O, Author
Woolfson, DN, Author
Sauer, G2, Author           
Dunin-Horkawicz, S1, Author           
Lupas, AN1, Author           
Hernandez Alvarez, B1, 3, Author           
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              
2Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society, Max-Planck-Ring 5, 72076 Tübingen, DE, ou_3375718              
3Conservation of Protein Structure and Function Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477389              

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 Abstract: Most core residues of coiled coils are hydrophobic. Occasional polar residues are thought to lower stability, but impart structural specificity. The coiled coils of trimeric autotransporter adhesins (TAAs) are conspicuous for their large number of polar residues in position d of the core, which often leads to their prediction as natively unstructured regions. The most frequent residue, asparagine (N@d), can occur in runs of up to 19 consecutive heptads, frequently in the motif [I/V]xxNTxx. In the Salmonella TAA, SadA, the core asparagines form rings of interacting residues with the following threonines, grouped around a central anion. This conformation is observed generally in N@d layers from trimeric coiled coils of known structure. Attempts to impose a different register on the motif show that the asparagines orient themselves specifically into the core, even against conflicting information from flanking domains. When engineered into the GCN4 leucine zipper, N@d layers progressively destabilized the structure, but zippers with 3 N@d layers still folded at high concentration. We propose that N@d layers maintain the coiled coils of TAAs in a soluble, export-competent state during autotransport through the outer membrane. More generally, we think that polar motifs that are both periodic and conserved may often reflect special folding requirements, rather than an unstructured state of the mature proteins.

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 Dates: 2009-10
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1073/pnas.0907256106
PMID: 19805097
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 106 (40) Sequence Number: - Start / End Page: 16950 - 16955 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230