3Q7X

Crystal structure of Symfoil-4P/PV1: de novo designed beta-trefoil architecture with symmetric primary structure, primitive version 1

Summary for 3Q7X

• Entry DOI: 10.2210/pdb3q7x/pdb
• Related: 1JQZ 3O4D 3Q7W 3Q7Y
• Descriptor: de novo designed beta-trefoil architecture with symmetric primary structure, SULFATE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: beta-trefoil, beta-terfoil, de novo protein
• Total number of polymer chains: 1
• Total formula weight: 14744.85

Authors

Blaber, M.,Lee, J. (deposition date: 2011-01-05, release date: 2012-01-11, Last modification date: 2024-02-21)

Primary citation

Longo, L.M.,Lee, J.,Blaber, M.
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein.
Proc.Natl.Acad.Sci.USA, 110:2135-2139, 2013

PubMed Abstract: 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.

PubMed: 23341608
DOI: 10.1073/pnas.1219530110

Experimental method

X-RAY DIFFRACTION (1.4 Å)