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PDBsum entry 4d8h
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De novo protein
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PDB id
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4d8h
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References listed in PDB file
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Key reference
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Title
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Simplified protein design biased for prebiotic amino acids yields a foldable, Halophilic protein.
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Authors
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L.M.Longo,
J.Lee,
M.Blaber.
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Ref.
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Proc Natl Acad Sci U S A, 2013,
110,
2135-2139.
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PubMed id
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Abstract
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A compendium of different types of abiotic chemical syntheses identifies a
consensus set of 10 "prebiotic" α-amino acids. Before the emergence
of biosynthetic pathways, this set is the most plausible resource for protein
formation (i.e., proteogenesis) within the overall process of abiogenesis. An
essential unsolved question regarding this prebiotic set is whether it defines a
"foldable set"-that is, does it contain sufficient chemical
information to permit cooperatively folding polypeptides? If so, what (if any)
characteristic properties might such polypeptides exhibit? To investigate these
questions, two "primitive" versions of an extant protein fold (the
β-trefoil) were produced by top-down symmetric deconstruction, resulting in a
reduced alphabet size of 12 or 13 amino acids and a percentage of prebiotic
amino acids approaching 80%. These proteins show a substantial acidification of
pI and require high salt concentrations for cooperative folding. The results
suggest that the prebiotic amino acids do comprise a foldable set within the
halophile environment.
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